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description Publicationkeyboard_double_arrow_right Article , Other literature type 2023 United KingdomPublisher:Proceedings of the National Academy of Sciences Funded by:UKRI | Elucidating the transient..., UKRI | Engineering new capacitie..., EC | PhotoRedesignUKRI| Elucidating the transient nature of electron transfer complexes at the single-molecule level ,UKRI| Engineering new capacities for solar energy utilisation in bacteria ,EC| PhotoRedesignAuthors: David J. K. Swainsbury; Frederick R. Hawkings; Elizabeth C. Martin; Sabina Musiał; +7 AuthorsDavid J. K. Swainsbury; Frederick R. Hawkings; Elizabeth C. Martin; Sabina Musiał; Jack H. Salisbury; Philip J. Jackson; David A. Farmer; Matthew P. Johnson; C. Alistair Siebert; Andrew Hitchcock; C. Neil Hunter;Cytochrome bc 1 complexes are ubiquinol:cytochrome c oxidoreductases, and as such, they are centrally important components of respiratory and photosynthetic electron transfer chains in many species of bacteria and in mitochondria. The minimal complex has three catalytic components, which are cytochrome b , cytochrome c 1 , and the Rieske iron–sulfur subunit, but the function of mitochondrial cytochrome bc 1 complexes is modified by up to eight supernumerary subunits. The cytochrome bc 1 complex from the purple phototrophic bacterium Rhodobacter sphaeroides has a single supernumerary subunit called subunit IV, which is absent from current structures of the complex. In this work we use the styrene–maleic acid copolymer to purify the R. sphaeroides cytochrome bc 1 complex in native lipid nanodiscs, which retains the labile subunit IV, annular lipids, and natively bound quinones. The catalytic activity of the four-subunit cytochrome bc 1 complex is threefold higher than that of the complex lacking subunit IV. To understand the role of subunit IV, we determined the structure of the four-subunit complex at 2.9 Å using single particle cryogenic electron microscopy. The structure shows the position of the transmembrane domain of subunit IV, which lies across the transmembrane helices of the Rieske and cytochrome c 1 subunits. We observe a quinone at the Q o quinone-binding site and show that occupancy of this site is linked to conformational changes in the Rieske head domain during catalysis. Twelve lipids were structurally resolved, making contacts with the Rieske and cytochrome b subunits, with some spanning both of the two monomers that make up the dimeric complex.
University of East A... arrow_drop_down University of East Anglia digital repositoryArticle . 2023 . Peer-reviewedLicense: CC BYData sources: University of East Anglia digital repositoryUniversity of East Anglia: UEA Digital RepositoryArticle . 2023License: CC BYData sources: Bielefeld Academic Search Engine (BASE)Proceedings of the National Academy of SciencesArticle . 2023 . Peer-reviewedLicense: CC BYData sources: CrossrefProceedings of the National Academy of SciencesArticle . 2023 . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1073/pnas.2217922120&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert University of East A... arrow_drop_down University of East Anglia digital repositoryArticle . 2023 . Peer-reviewedLicense: CC BYData sources: University of East Anglia digital repositoryUniversity of East Anglia: UEA Digital RepositoryArticle . 2023License: CC BYData sources: Bielefeld Academic Search Engine (BASE)Proceedings of the National Academy of SciencesArticle . 2023 . Peer-reviewedLicense: CC BYData sources: CrossrefProceedings of the National Academy of SciencesArticle . 2023 . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1073/pnas.2217922120&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Journal 2019 United KingdomPublisher:Elsevier BV Funded by:UKRI | Quantification of the for..., EC | SYNTHPHOTO, UKRI | Engineering new capacitie...UKRI| Quantification of the forces that mediate electron transfers between proteins ,EC| SYNTHPHOTO ,UKRI| Engineering new capacities for solar energy utilisation in bacteriaMayneord, G.E.; Vasilev, C.; Malone, L.A.; Swainsbury, D.J.K.; Hunter, C.N.; Johnson, M.P.;pmid: 31247170
Small diffusible redox proteins play a ubiquitous role in bioenergetic systems, facilitating electron transfer (ET) between membrane bound complexes. Sustaining high ET turnover rates requires that the association between extrinsic and membrane-bound partners is highly specific, yet also sufficiently weak to promote rapid post-ET separation. In oxygenic photosynthesis the small soluble electron carrier protein plastocyanin (Pc) shuttles electrons between the membrane integral cytochrome b6f (cytb6f) and photosystem I (PSI) complexes. Here we use peak-force quantitative nanomechanical mapping (PF-QNM) atomic force microscopy (AFM) to quantify the dynamic forces involved in transient interactions between cognate ET partners. An AFM probe functionalised with Pc molecules is brought into contact with cytb6f complexes, immobilised on a planar silicon surface. PF-QNM interrogates the unbinding force of the cytb6f-Pc interactions at the single molecule level with picoNewton force resolution and on a time scale comparable to the ET time in vivo (ca. 120 μs). Using this approach, we show that although the unbinding force remains unchanged the interaction frequency increases over five-fold when Pc and cytb6f are in opposite redox states, so complementary charges on the cytb6f and Pc cofactors likely contribute to the electrostatic forces that initiate formation of the ET complex. These results suggest that formation of the docking interface is under redox state control, which lowers the probability of unproductive encounters between Pc and cytb6f molecules in the same redox state, ensuring the efficiency and directionality of this central reaction in the 'Z-scheme' of photosynthetic ET.
Biochimica et Biophy... arrow_drop_down Biochimica et Biophysica Acta (BBA) - BioenergeticsArticleLicense: Elsevier Non-CommercialData sources: UnpayWallBiochimica et Biophysica Acta (BBA) - BioenergeticsArticle . 2019 . Peer-reviewedLicense: Elsevier Non-CommercialData sources: Crossrefhttp://dx.doi.org/10.1016/j.bb...Article . Peer-reviewedData sources: European Union Open Data PortalUniversity of East Anglia: UEA Digital RepositoryArticle . 2019Data sources: Bielefeld Academic Search Engine (BASE)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1016/j.bbabio.2019.06.013&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert Biochimica et Biophy... arrow_drop_down Biochimica et Biophysica Acta (BBA) - BioenergeticsArticleLicense: Elsevier Non-CommercialData sources: UnpayWallBiochimica et Biophysica Acta (BBA) - BioenergeticsArticle . 2019 . Peer-reviewedLicense: Elsevier Non-CommercialData sources: Crossrefhttp://dx.doi.org/10.1016/j.bb...Article . Peer-reviewedData sources: European Union Open Data PortalUniversity of East Anglia: UEA Digital RepositoryArticle . 2019Data sources: Bielefeld Academic Search Engine (BASE)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1016/j.bbabio.2019.06.013&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Other literature type 2022Embargo end date: 21 Mar 2023 GermanyPublisher:American Association for the Advancement of Science (AAAS) Funded by:UKRI | Engineering new capacitie..., UKRI | NITROPLAST: A LIGHT-DRIVE..., EC | PhotoRedesign +5 projectsUKRI| Engineering new capacities for solar energy utilisation in bacteria ,UKRI| NITROPLAST: A LIGHT-DRIVEN, SYNTHETIC NITROGEN-FIXING ORGANELLE ,EC| PhotoRedesign ,UKRI| Chlorophyll-f-containing Photosystem I ,NSF| GLOBEC: Collaborative Research: Mesoscale and Finescale Mapping of Physical and Biological Fields in the Northern California Current System ,UKRI| Photosynthetic water oxidation driven by near infra-red light ,UKRI| Mass spectrometry underpinning synthetic biology, industrial biotechnology and world class bioscience ,UKRI| Elucidating the transient nature of electron transfer complexes at the single-molecule levelAuthors: MacGregor-Chatwin, Craig; Nürnberg, Dennis J.; Jackson, Philip J.; Vasilev, Cvetelin; +12 AuthorsMacGregor-Chatwin, Craig; Nürnberg, Dennis J.; Jackson, Philip J.; Vasilev, Cvetelin; Hitchcock, Andrew; Ho, Ming-Yang; Shen, Gaozhong; Gisriel, Christopher J.; Wood, William H.J.; Mahbub, Moontaha; Selinger, Vera M.; Johnson, Matthew P.; Dickman, Mark J.; Rutherford, Alfred William; Bryant, Donald A.; Hunter, C. Neil;Cyanobacteria are ubiquitous in nature and have developed numerous strategies that allow them to live in a diverse range of environments. Certain cyanobacteria synthesize chlorophylls d and f to acclimate to niches enriched in far-red light (FRL) and incorporate paralogous photosynthetic proteins into their photosynthetic apparatus in a process called FRL-induced photoacclimation (FaRLiP). We characterized the macromolecular changes involved in FRL-driven photosynthesis and used atomic force microscopy to examine the supramolecular organization of photosystem I associated with FaRLiP in three cyanobacterial species. Mass spectrometry showed the changes in the proteome of Chroococcidiopsis thermalis PCC 7203 that accompany FaRLiP. Fluorescence lifetime imaging microscopy and electron microscopy reveal an altered cellular distribution of photosystem complexes and illustrate the cell-to-cell variability of the FaRLiP response.
Science Advances arrow_drop_down Refubium - Repositorium der Freien Universität BerlinArticle . 2022License: CC BYData sources: Refubium - Repositorium der Freien Universität Berlinadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1126/sciadv.abj4437&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert Science Advances arrow_drop_down Refubium - Repositorium der Freien Universität BerlinArticle . 2022License: CC BYData sources: Refubium - Repositorium der Freien Universität Berlinadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1126/sciadv.abj4437&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Other literature type , Journal 2018 United KingdomPublisher:Elsevier BV Funded by:EC | SYNTHPHOTO, UKRI | Engineering new capacitie..., UKRI | Artificial thylakoids: a ...EC| SYNTHPHOTO ,UKRI| Engineering new capacities for solar energy utilisation in bacteria ,UKRI| Artificial thylakoids: a bio-inspired platform for investigating assembly and organization in multi-layer membranesAuthors: Adams, P.G.; Vasilev, C.; Hunter, C.N.; Johnson, M.P.;Light-Harvesting Complex II (LHCII) is a chlorophyll-protein antenna complex that efficiently absorbs solar energy and transfers electronic excited states to photosystems I and II. Under excess light intensity LHCII can adopt a photoprotective state in which excitation energy is safely dissipated as heat, a process known as Non-Photochemical Quenching (NPQ). In vivo NPQ is triggered by combinatorial factors including transmembrane ΔpH, PsbS protein and LHCII-bound zeaxanthin, leading to dramatically shortened LHCII fluorescence lifetimes. In vitro, LHCII in detergent solution or in proteoliposomes can reversibly adopt an NPQ-like state, via manipulation of detergent/protein ratio, lipid/protein ratio, pH or pressure. Previous spectroscopic investigations revealed changes in exciton dynamics and protein conformation that accompany quenching, however, LHCII-LHCII interactions have not been extensively studied. Here, we correlated fluorescence lifetime imaging microscopy (FLIM) and atomic force microscopy (AFM) of trimeric LHCII adsorbed to mica substrates and manipulated the environment to cause varying degrees of quenching. AFM showed that LHCII self-assembled onto mica forming 2D-aggregates (25-150 nm width). FLIM determined that LHCII in these aggregates were in a quenched state, with much lower fluorescence lifetimes (~0.25 ns) compared to free LHCII in solution (2.2-3.9 ns). LHCII-LHCII interactions were disrupted by thylakoid lipids or phospholipids, leading to intermediate fluorescent lifetimes (0.6-0.9 ns). To our knowledge, this is the first in vitro correlation of nanoscale membrane imaging with LHCII quenching. Our findings suggest that lipids could play a key role in modulating the extent of LHCII-LHCII interactions within the thylakoid membrane and so the propensity for NPQ activation.
CORE arrow_drop_down Biochimica et Biophysica Acta (BBA) - BioenergeticsArticle . 2018 . Peer-reviewedLicense: CC BYData sources: Crossrefhttp://dx.doi.org/10.1016/j.bb...Article . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1016/j.bbabio.2018.06.011&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert CORE arrow_drop_down Biochimica et Biophysica Acta (BBA) - BioenergeticsArticle . 2018 . Peer-reviewedLicense: CC BYData sources: Crossrefhttp://dx.doi.org/10.1016/j.bb...Article . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1016/j.bbabio.2018.06.011&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Other literature type , Journal 2019 United KingdomPublisher:Portland Press Ltd. Funded by:UKRI | Engineering new capacitie..., UKRI | Quantification of the for..., EC | SYNTHPHOTOUKRI| Engineering new capacities for solar energy utilisation in bacteria ,UKRI| Quantification of the forces that mediate electron transfers between proteins ,EC| SYNTHPHOTOVasilev, C.; Mayneord, G.E.; Brindley, A.A.; Johnson, M.P.; Hunter, C.N.;Abstract The reversible docking of small, diffusible redox proteins onto a membrane protein complex is a common feature of bacterial, mitochondrial and photosynthetic electron transfer (ET) chains. Spectroscopic studies of ensembles of such redox partners have been used to determine ET rates and dissociation constants. Here, we report a single-molecule analysis of the forces that stabilise transient ET complexes. We examined the interaction of two components of bacterial photosynthesis, cytochrome c2 and the reaction centre (RC) complex, using dynamic force spectroscopy and PeakForce quantitative nanomechanical imaging. RC–LH1–PufX complexes, attached to silicon nitride AFM probes and maintained in a photo-oxidised state, were lowered onto a silicon oxide substrate bearing dispersed, immobilised and reduced cytochrome c2 molecules. Microscale patterns of cytochrome c2 and the cyan fluorescent protein were used to validate the specificity of recognition between tip-attached RCs and surface-tethered cytochrome c2. Following the transient association of photo-oxidised RC and reduced cytochrome c2 molecules, retraction of the RC-functionalised probe met with resistance, and forces between 112 and 887 pN were required to disrupt the post-ET RC–c2 complex, depending on the retraction velocities used. If tip-attached RCs were reduced instead, the probability of interaction with reduced cytochrome c2 molecules decreased 5-fold. Thus, the redox states of the cytochrome c2 haem cofactor and RC ‘special pair’ bacteriochlorophyll dimer are important for establishing a productive ET complex. The millisecond persistence of the post-ET cytochrome c2[oxidised]–RC[reduced] ‘product’ state is compatible with rates of cyclic photosynthetic ET, at physiologically relevant light intensities.
Biochemical Journal arrow_drop_down http://dx.doi.org/10.1042/BCJ2...Article . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1042/bcj20170519&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert Biochemical Journal arrow_drop_down http://dx.doi.org/10.1042/BCJ2...Article . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1042/bcj20170519&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Journal 2020Publisher:Portland Press Ltd. Funded by:UKRI | Mass spectrometry underpi..., EC | PhotoRedesign, UKRI | Engineering new capacitie...UKRI| Mass spectrometry underpinning synthetic biology, industrial biotechnology and world class bioscience ,EC| PhotoRedesign ,UKRI| Engineering new capacities for solar energy utilisation in bacteriaMatthew P. Johnson; Elizabeth C. Martin; Andrew Hitchcock; Matthew S. Proctor; Jan Pilný; Philip J. Jackson; Marek Pazderník; Marek Pazderník; Roman Sobotka; Roman Sobotka; Mark J. Dickman; C. Neil Hunter; Daniel P. Canniffe;doi: 10.1042/bcj20200561
pmid: 32990304
Chlorophyll synthase (ChlG) catalyses a terminal reaction in the chlorophyll biosynthesis pathway, attachment of phytol or geranylgeraniol to the C17 propionate of chlorophyllide. Cyanobacterial ChlG forms a stable complex with high light-inducible protein D (HliD), a small single-helix protein homologous to the third transmembrane helix of plant light-harvesting complexes (LHCs). The ChlG–HliD assembly binds chlorophyll, β-carotene, zeaxanthin and myxoxanthophyll and associates with the YidC insertase, most likely to facilitate incorporation of chlorophyll into translated photosystem apoproteins. HliD independently coordinates chlorophyll and β-carotene but the role of the xanthophylls, which appear to be exclusive to the core ChlG–HliD assembly, is unclear. Here we generated mutants of Synechocystis sp. PCC 6803 lacking specific combinations of carotenoids or HliD in a background with FLAG- or His-tagged ChlG. Immunoprecipitation experiments and analysis of isolated membranes demonstrate that the absence of zeaxanthin and myxoxanthophyll significantly weakens the interaction between HliD and ChlG. ChlG alone does not bind carotenoids and accumulation of the chlorophyllide substrate in the absence of xanthophylls indicates that activity/stability of the ‘naked’ enzyme is perturbed. In contrast, the interaction of HliD with a second partner, the photosystem II assembly factor Ycf39, is preserved in the absence of xanthophylls. We propose that xanthophylls are required for the stable association of ChlG and HliD, acting as a ‘molecular glue’ at the lateral transmembrane interface between these proteins; roles for zeaxanthin and myxoxanthophyll in ChlG–HliD complexation are discussed, as well as the possible presence of similar complexes between LHC-like proteins and chlorophyll biosynthesis enzymes in plants.
CORE arrow_drop_down add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1042/bcj20200561&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert CORE arrow_drop_down add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1042/bcj20200561&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Journal 2022 United KingdomPublisher:Elsevier BV Funded by:UKRI | Sheffield antimicrobial r..., UKRI | Engineering new capacitie..., UKRI | Elucidating the transient... +2 projectsUKRI| Sheffield antimicrobial resistance network - SHAMROK ,UKRI| Engineering new capacities for solar energy utilisation in bacteria ,UKRI| Elucidating the transient nature of electron transfer complexes at the single-molecule level ,UKRI| Quantification of the forces that mediate electron transfers between proteins ,EC| PhotoRedesignVasilev, C.; Swainsbury, D.J.K.; Cartron, M.L.; Martin, E.C.; Kumar, S.; Hobbs, J.K.; Johnson, M.P.; Hitchcock, A.; Hunter, C.N.;pmid: 34793767
In the model purple phototrophic bacterium Rhodobacter (Rba.) sphaeroides, solar energy is converted via coupled electron and proton transfer reactions within the intracytoplasmic membranes (ICMs), infoldings of the cytoplasmic membrane that form spherical 'chromatophore' vesicles. These bacterial 'organelles' are ideal model systems for studying how the organisation of the photosynthetic complexes therein shape membrane architecture. In Rba. sphaeroides, light-harvesting 2 (LH2) complexes transfer absorbed excitation energy to dimeric reaction centre (RC)-LH1-PufX complexes. The PufX polypeptide creates a channel that allows the lipid soluble electron carrier quinol, produced by RC photochemistry, to diffuse to the cytochrome bc1 complex, where quinols are oxidised to quinones, with the liberated protons used to generate a transmembrane proton gradient and the electrons returned to the RC via cytochrome c2. Proximity between cytochrome bc1 and RC-LH1-PufX minimises quinone/quinol/cytochrome c2 diffusion distances within this protein-crowded membrane, however this distance has not yet been measured. Here, we tag the RC and cytochrome bc1 with yellow or cyan fluorescent proteins (YFP/CFP) and record the lifetimes of YFP/CFP Förster resonance energy transfer (FRET) pairs in whole cells. FRET analysis shows that that these complexes lie on average within 6 nm of each other. Complementary high-resolution atomic force microscopy (AFM) of intact, purified chromatophores verifies the close association of cytochrome bc1 complexes with RC-LH1-PufX dimers. Our results provide a structural basis for the close kinetic coupling between RC-LH1-PufX and cytochrome bc1 observed by spectroscopy, and explain how quinols/quinones and cytochrome c2 shuttle on a millisecond timescale between these complexes, sustaining efficient photosynthetic electron flow.
CORE arrow_drop_down CORE (RIOXX-UK Aggregator)Article . 2022License: CC BY NC NDData sources: CORE (RIOXX-UK Aggregator)Biochimica et Biophysica Acta (BBA) - BioenergeticsArticle . 2022 . Peer-reviewedLicense: Elsevier Non-CommercialData sources: CrossrefBiochimica et Biophysica ActaArticle . 2022 . Peer-reviewedData sources: European Union Open Data PortalUniversity of East Anglia: UEA Digital RepositoryArticle . 2022Data sources: Bielefeld Academic Search Engine (BASE)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1016/j.bbabio.2021.148508&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert CORE arrow_drop_down CORE (RIOXX-UK Aggregator)Article . 2022License: CC BY NC NDData sources: CORE (RIOXX-UK Aggregator)Biochimica et Biophysica Acta (BBA) - BioenergeticsArticle . 2022 . Peer-reviewedLicense: Elsevier Non-CommercialData sources: CrossrefBiochimica et Biophysica ActaArticle . 2022 . Peer-reviewedData sources: European Union Open Data PortalUniversity of East Anglia: UEA Digital RepositoryArticle . 2022Data sources: Bielefeld Academic Search Engine (BASE)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1016/j.bbabio.2021.148508&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Journal 2019 United KingdomPublisher:Oxford University Press (OUP) Funded by:UKRI | Engineering new capacitie...UKRI| Engineering new capacities for solar energy utilisation in bacteriaWilliam H.J. Wood; Samuel F.H. Barnett; Sarah Flannery; C. Neil Hunter; Matthew P. Johnson;doi: 10.1104/pp.19.00503
Grana stacking in plant chloroplast thylakoid membranes dynamically responds to the light environment. These dynamics have been linked to regulation of the relative antenna sizes of PSI and PSII (state transitions), the PSII repair cycle, and the regulation of photosynthetic electron transfer. Here, we used 3D structured illumination microscopy, a subdiffraction-resolution fluorescence imaging technique, to investigate the light-intensity dependence, kinetics, reversibility, and regulation of dynamic thylakoid stacking in spinach (Spinacia oleracea) and Arabidopsis (Arabidopsis thaliana). Low-intensity white light (150 μmol photons m−2 s−1) behaved similarly to light preferentially exciting PSII (660 nm), causing a reduction in grana diameter and an increased number of grana per chloroplast. By contrast, high-intensity white light (1000 μmol photons m−2 s−1), darkness, and light preferentially exciting PSI (730 nm) reversed these changes. These dynamics occurred with a half-time of 7 to 8 min and were accompanied by state transitions. Consistent with this, the dynamics were dependent on STN7 (light-harvesting complex II [LHCII] kinase) and TAP38 (LHCII phosphatase), which are required for state transitions but were unaffected by the absence of STN8 (PSII kinase) or PSII core phosphatase (PSII phosphatase). Unlike state transitions, however, thylakoid stacking dynamics did not rely on the presence of the LHCI and PSI subunit L phospho-LHCII binding sites on PSI. Since oligomerization of thylakoid curvature protein (CURT1A) was unaffected by the absence of STN7 or TAP38, we conclude that the primary determinant of dynamic thylakoid stacking is LHCII phosphorylation.
PLANT PHYSIOLOGY arrow_drop_down add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1104/pp.19.00503&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert PLANT PHYSIOLOGY arrow_drop_down add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1104/pp.19.00503&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Other literature type , Journal 2019 United KingdomPublisher:Springer Science and Business Media LLC Funded by:UKRI | Engineering new capacitie..., UKRI | Quantification of the for..., NIH | Center for Macromolecular... +3 projectsUKRI| Engineering new capacities for solar energy utilisation in bacteria ,UKRI| Quantification of the forces that mediate electron transfers between proteins ,NIH| Center for Macromolecular Modeling and Bioinformatics ,UKRI| Mass spectrometry underpinning synthetic biology, industrial biotechnology and world class bioscience ,EC| SYNTHPHOTO ,UKRI| Revealing a mechanistic understanding of the role of viruses and host nutrient status in modulating CO2 fixation in key marine phototrophsC. MacGregor-Chatwin; P. J. Jackson; M. Sener; J. W. Chidgey; A. Hitchcock; P. Qian; G. E. Mayneord; M. P. Johnson; Z. Luthey-Schulten; M. J. Dickman; D. J. Scanlan; C. N. Hunter;Prochlorococcus is a major contributor to primary production, and globally the most abundant photosynthetic genus of picocyanobacteria because it can adapt to highly stratified low-nutrient conditions that are characteristic of the surface ocean. Here, we examine the structural adaptations of the photosynthetic thylakoid membrane that enable different Prochlorococcus ecotypes to occupy high-light, low-light and nutrient-poor ecological niches. We used atomic force microscopy to image the different photosystem I (PSI) membrane architectures of the MED4 (high-light) Prochlorococcus ecotype grown under high-light and low-light conditions in addition to the MIT9313 (low-light) and SS120 (low-light) Prochlorococcus ecotypes grown under low-light conditions. Mass spectrometry quantified the relative abundance of PSI, photosystem II (PSII) and cytochrome b6f complexes and the various Pcb proteins in the thylakoid membrane. Atomic force microscopy topographs and structural modelling revealed a series of specialized PSI configurations, each adapted to the environmental niche occupied by a particular ecotype. MED4 PSI domains were loosely packed in the thylakoid membrane, whereas PSI in the low-light MIT9313 is organized into a tightly packed pseudo-hexagonal lattice that maximizes harvesting and trapping of light. There are approximately equal levels of PSI and PSII in MED4 and MIT9313, but nearly twofold more PSII than PSI in SS120, which also has a lower content of cytochrome b6f complexes. SS120 has a different tactic to cope with low-light levels, and SS120 thylakoids contained hundreds of closely packed Pcb-PSI supercomplexes that economize on the extra iron and nitrogen required to assemble PSI-only domains. Thus, the abundance and widespread distribution of Prochlorococcus reflect the strategies that various ecotypes employ for adapting to limitations in light and nutrient levels.
CORE arrow_drop_down http://dx.doi.org/10.1038/s414...Article . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1038/s41477-019-0475-z&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert CORE arrow_drop_down http://dx.doi.org/10.1038/s414...Article . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1038/s41477-019-0475-z&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Other literature type , Journal 2020Publisher:Wiley Funded by:UKRI | Mass spectrometry underpi..., UKRI | SHeffield IMAging (SHIMA), UKRI | Engineering new capacitie...UKRI| Mass spectrometry underpinning synthetic biology, industrial biotechnology and world class bioscience ,UKRI| SHeffield IMAging (SHIMA) ,UKRI| Engineering new capacities for solar energy utilisation in bacteriaAuthors: Sarah E. Flannery; Christopher Hepworth; William H. J. Wood; Federica Pastorelli; +4 AuthorsSarah E. Flannery; Christopher Hepworth; William H. J. Wood; Federica Pastorelli; Christopher N. Hunter; Mark J. Dickman; Philip J. Jackson; Matthew P. Johnson;SummaryPhotosynthetic acclimation, the ability to adjust the composition of the thylakoid membrane to optimise the efficiency of electron transfer to the prevailing light conditions, is crucial to plant fitness in the field. While much is known about photosynthetic acclimation in Arabidopsis, to date there has been no study that combines both quantitative label‐free proteomics and photosynthetic analysis by gas exchange, chlorophyll fluorescence and P700 absorption spectroscopy. Using these methods we investigated how the levels of 402 thylakoid proteins, including many regulatory proteins not previously quantified, varied upon long‐term (weeks) acclimation of Arabidopsis to low (LL), moderate (ML) and high (HL) growth light intensity and correlated these with key photosynthetic parameters. We show that changes in the relative abundance of cytb6f, ATP synthase, FNR2, TIC62 and PGR6 positively correlate with changes in estimated PSII electron transfer rate and CO2 assimilation. Improved photosynthetic capacity in HL grown plants is paralleled by increased cyclic electron transport, which positively correlated with NDH, PGRL1, FNR1, FNR2 and TIC62, although not PGR5 abundance. The photoprotective acclimation strategy was also contrasting, with LL plants favouring slowly reversible non‐photochemical quenching (qI), which positively correlated with LCNP, while HL plants favoured rapidly reversible quenching (qE), which positively correlated with PSBS. The long‐term adjustment of thylakoid membrane grana diameter positively correlated with LHCII levels, while grana stacking negatively correlated with CURT1 and RIQ protein abundance. The data provide insights into how Arabidopsis tunes photosynthetic electron transfer and its regulation during developmental acclimation to light intensity.
add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1111/tpj.15053&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
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description Publicationkeyboard_double_arrow_right Article , Other literature type 2023 United KingdomPublisher:Proceedings of the National Academy of Sciences Funded by:UKRI | Elucidating the transient..., UKRI | Engineering new capacitie..., EC | PhotoRedesignUKRI| Elucidating the transient nature of electron transfer complexes at the single-molecule level ,UKRI| Engineering new capacities for solar energy utilisation in bacteria ,EC| PhotoRedesignAuthors: David J. K. Swainsbury; Frederick R. Hawkings; Elizabeth C. Martin; Sabina Musiał; +7 AuthorsDavid J. K. Swainsbury; Frederick R. Hawkings; Elizabeth C. Martin; Sabina Musiał; Jack H. Salisbury; Philip J. Jackson; David A. Farmer; Matthew P. Johnson; C. Alistair Siebert; Andrew Hitchcock; C. Neil Hunter;Cytochrome bc 1 complexes are ubiquinol:cytochrome c oxidoreductases, and as such, they are centrally important components of respiratory and photosynthetic electron transfer chains in many species of bacteria and in mitochondria. The minimal complex has three catalytic components, which are cytochrome b , cytochrome c 1 , and the Rieske iron–sulfur subunit, but the function of mitochondrial cytochrome bc 1 complexes is modified by up to eight supernumerary subunits. The cytochrome bc 1 complex from the purple phototrophic bacterium Rhodobacter sphaeroides has a single supernumerary subunit called subunit IV, which is absent from current structures of the complex. In this work we use the styrene–maleic acid copolymer to purify the R. sphaeroides cytochrome bc 1 complex in native lipid nanodiscs, which retains the labile subunit IV, annular lipids, and natively bound quinones. The catalytic activity of the four-subunit cytochrome bc 1 complex is threefold higher than that of the complex lacking subunit IV. To understand the role of subunit IV, we determined the structure of the four-subunit complex at 2.9 Å using single particle cryogenic electron microscopy. The structure shows the position of the transmembrane domain of subunit IV, which lies across the transmembrane helices of the Rieske and cytochrome c 1 subunits. We observe a quinone at the Q o quinone-binding site and show that occupancy of this site is linked to conformational changes in the Rieske head domain during catalysis. Twelve lipids were structurally resolved, making contacts with the Rieske and cytochrome b subunits, with some spanning both of the two monomers that make up the dimeric complex.
University of East A... arrow_drop_down University of East Anglia digital repositoryArticle . 2023 . Peer-reviewedLicense: CC BYData sources: University of East Anglia digital repositoryUniversity of East Anglia: UEA Digital RepositoryArticle . 2023License: CC BYData sources: Bielefeld Academic Search Engine (BASE)Proceedings of the National Academy of SciencesArticle . 2023 . Peer-reviewedLicense: CC BYData sources: CrossrefProceedings of the National Academy of SciencesArticle . 2023 . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1073/pnas.2217922120&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert University of East A... arrow_drop_down University of East Anglia digital repositoryArticle . 2023 . Peer-reviewedLicense: CC BYData sources: University of East Anglia digital repositoryUniversity of East Anglia: UEA Digital RepositoryArticle . 2023License: CC BYData sources: Bielefeld Academic Search Engine (BASE)Proceedings of the National Academy of SciencesArticle . 2023 . Peer-reviewedLicense: CC BYData sources: CrossrefProceedings of the National Academy of SciencesArticle . 2023 . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1073/pnas.2217922120&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Journal 2019 United KingdomPublisher:Elsevier BV Funded by:UKRI | Quantification of the for..., EC | SYNTHPHOTO, UKRI | Engineering new capacitie...UKRI| Quantification of the forces that mediate electron transfers between proteins ,EC| SYNTHPHOTO ,UKRI| Engineering new capacities for solar energy utilisation in bacteriaMayneord, G.E.; Vasilev, C.; Malone, L.A.; Swainsbury, D.J.K.; Hunter, C.N.; Johnson, M.P.;pmid: 31247170
Small diffusible redox proteins play a ubiquitous role in bioenergetic systems, facilitating electron transfer (ET) between membrane bound complexes. Sustaining high ET turnover rates requires that the association between extrinsic and membrane-bound partners is highly specific, yet also sufficiently weak to promote rapid post-ET separation. In oxygenic photosynthesis the small soluble electron carrier protein plastocyanin (Pc) shuttles electrons between the membrane integral cytochrome b6f (cytb6f) and photosystem I (PSI) complexes. Here we use peak-force quantitative nanomechanical mapping (PF-QNM) atomic force microscopy (AFM) to quantify the dynamic forces involved in transient interactions between cognate ET partners. An AFM probe functionalised with Pc molecules is brought into contact with cytb6f complexes, immobilised on a planar silicon surface. PF-QNM interrogates the unbinding force of the cytb6f-Pc interactions at the single molecule level with picoNewton force resolution and on a time scale comparable to the ET time in vivo (ca. 120 μs). Using this approach, we show that although the unbinding force remains unchanged the interaction frequency increases over five-fold when Pc and cytb6f are in opposite redox states, so complementary charges on the cytb6f and Pc cofactors likely contribute to the electrostatic forces that initiate formation of the ET complex. These results suggest that formation of the docking interface is under redox state control, which lowers the probability of unproductive encounters between Pc and cytb6f molecules in the same redox state, ensuring the efficiency and directionality of this central reaction in the 'Z-scheme' of photosynthetic ET.
Biochimica et Biophy... arrow_drop_down Biochimica et Biophysica Acta (BBA) - BioenergeticsArticleLicense: Elsevier Non-CommercialData sources: UnpayWallBiochimica et Biophysica Acta (BBA) - BioenergeticsArticle . 2019 . Peer-reviewedLicense: Elsevier Non-CommercialData sources: Crossrefhttp://dx.doi.org/10.1016/j.bb...Article . Peer-reviewedData sources: European Union Open Data PortalUniversity of East Anglia: UEA Digital RepositoryArticle . 2019Data sources: Bielefeld Academic Search Engine (BASE)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1016/j.bbabio.2019.06.013&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert Biochimica et Biophy... arrow_drop_down Biochimica et Biophysica Acta (BBA) - BioenergeticsArticleLicense: Elsevier Non-CommercialData sources: UnpayWallBiochimica et Biophysica Acta (BBA) - BioenergeticsArticle . 2019 . Peer-reviewedLicense: Elsevier Non-CommercialData sources: Crossrefhttp://dx.doi.org/10.1016/j.bb...Article . Peer-reviewedData sources: European Union Open Data PortalUniversity of East Anglia: UEA Digital RepositoryArticle . 2019Data sources: Bielefeld Academic Search Engine (BASE)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1016/j.bbabio.2019.06.013&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Other literature type 2022Embargo end date: 21 Mar 2023 GermanyPublisher:American Association for the Advancement of Science (AAAS) Funded by:UKRI | Engineering new capacitie..., UKRI | NITROPLAST: A LIGHT-DRIVE..., EC | PhotoRedesign +5 projectsUKRI| Engineering new capacities for solar energy utilisation in bacteria ,UKRI| NITROPLAST: A LIGHT-DRIVEN, SYNTHETIC NITROGEN-FIXING ORGANELLE ,EC| PhotoRedesign ,UKRI| Chlorophyll-f-containing Photosystem I ,NSF| GLOBEC: Collaborative Research: Mesoscale and Finescale Mapping of Physical and Biological Fields in the Northern California Current System ,UKRI| Photosynthetic water oxidation driven by near infra-red light ,UKRI| Mass spectrometry underpinning synthetic biology, industrial biotechnology and world class bioscience ,UKRI| Elucidating the transient nature of electron transfer complexes at the single-molecule levelAuthors: MacGregor-Chatwin, Craig; Nürnberg, Dennis J.; Jackson, Philip J.; Vasilev, Cvetelin; +12 AuthorsMacGregor-Chatwin, Craig; Nürnberg, Dennis J.; Jackson, Philip J.; Vasilev, Cvetelin; Hitchcock, Andrew; Ho, Ming-Yang; Shen, Gaozhong; Gisriel, Christopher J.; Wood, William H.J.; Mahbub, Moontaha; Selinger, Vera M.; Johnson, Matthew P.; Dickman, Mark J.; Rutherford, Alfred William; Bryant, Donald A.; Hunter, C. Neil;Cyanobacteria are ubiquitous in nature and have developed numerous strategies that allow them to live in a diverse range of environments. Certain cyanobacteria synthesize chlorophylls d and f to acclimate to niches enriched in far-red light (FRL) and incorporate paralogous photosynthetic proteins into their photosynthetic apparatus in a process called FRL-induced photoacclimation (FaRLiP). We characterized the macromolecular changes involved in FRL-driven photosynthesis and used atomic force microscopy to examine the supramolecular organization of photosystem I associated with FaRLiP in three cyanobacterial species. Mass spectrometry showed the changes in the proteome of Chroococcidiopsis thermalis PCC 7203 that accompany FaRLiP. Fluorescence lifetime imaging microscopy and electron microscopy reveal an altered cellular distribution of photosystem complexes and illustrate the cell-to-cell variability of the FaRLiP response.
Science Advances arrow_drop_down Refubium - Repositorium der Freien Universität BerlinArticle . 2022License: CC BYData sources: Refubium - Repositorium der Freien Universität Berlinadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1126/sciadv.abj4437&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert Science Advances arrow_drop_down Refubium - Repositorium der Freien Universität BerlinArticle . 2022License: CC BYData sources: Refubium - Repositorium der Freien Universität Berlinadd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1126/sciadv.abj4437&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Other literature type , Journal 2018 United KingdomPublisher:Elsevier BV Funded by:EC | SYNTHPHOTO, UKRI | Engineering new capacitie..., UKRI | Artificial thylakoids: a ...EC| SYNTHPHOTO ,UKRI| Engineering new capacities for solar energy utilisation in bacteria ,UKRI| Artificial thylakoids: a bio-inspired platform for investigating assembly and organization in multi-layer membranesAuthors: Adams, P.G.; Vasilev, C.; Hunter, C.N.; Johnson, M.P.;Light-Harvesting Complex II (LHCII) is a chlorophyll-protein antenna complex that efficiently absorbs solar energy and transfers electronic excited states to photosystems I and II. Under excess light intensity LHCII can adopt a photoprotective state in which excitation energy is safely dissipated as heat, a process known as Non-Photochemical Quenching (NPQ). In vivo NPQ is triggered by combinatorial factors including transmembrane ΔpH, PsbS protein and LHCII-bound zeaxanthin, leading to dramatically shortened LHCII fluorescence lifetimes. In vitro, LHCII in detergent solution or in proteoliposomes can reversibly adopt an NPQ-like state, via manipulation of detergent/protein ratio, lipid/protein ratio, pH or pressure. Previous spectroscopic investigations revealed changes in exciton dynamics and protein conformation that accompany quenching, however, LHCII-LHCII interactions have not been extensively studied. Here, we correlated fluorescence lifetime imaging microscopy (FLIM) and atomic force microscopy (AFM) of trimeric LHCII adsorbed to mica substrates and manipulated the environment to cause varying degrees of quenching. AFM showed that LHCII self-assembled onto mica forming 2D-aggregates (25-150 nm width). FLIM determined that LHCII in these aggregates were in a quenched state, with much lower fluorescence lifetimes (~0.25 ns) compared to free LHCII in solution (2.2-3.9 ns). LHCII-LHCII interactions were disrupted by thylakoid lipids or phospholipids, leading to intermediate fluorescent lifetimes (0.6-0.9 ns). To our knowledge, this is the first in vitro correlation of nanoscale membrane imaging with LHCII quenching. Our findings suggest that lipids could play a key role in modulating the extent of LHCII-LHCII interactions within the thylakoid membrane and so the propensity for NPQ activation.
CORE arrow_drop_down Biochimica et Biophysica Acta (BBA) - BioenergeticsArticle . 2018 . Peer-reviewedLicense: CC BYData sources: Crossrefhttp://dx.doi.org/10.1016/j.bb...Article . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1016/j.bbabio.2018.06.011&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert CORE arrow_drop_down Biochimica et Biophysica Acta (BBA) - BioenergeticsArticle . 2018 . Peer-reviewedLicense: CC BYData sources: Crossrefhttp://dx.doi.org/10.1016/j.bb...Article . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1016/j.bbabio.2018.06.011&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Other literature type , Journal 2019 United KingdomPublisher:Portland Press Ltd. Funded by:UKRI | Engineering new capacitie..., UKRI | Quantification of the for..., EC | SYNTHPHOTOUKRI| Engineering new capacities for solar energy utilisation in bacteria ,UKRI| Quantification of the forces that mediate electron transfers between proteins ,EC| SYNTHPHOTOVasilev, C.; Mayneord, G.E.; Brindley, A.A.; Johnson, M.P.; Hunter, C.N.;Abstract The reversible docking of small, diffusible redox proteins onto a membrane protein complex is a common feature of bacterial, mitochondrial and photosynthetic electron transfer (ET) chains. Spectroscopic studies of ensembles of such redox partners have been used to determine ET rates and dissociation constants. Here, we report a single-molecule analysis of the forces that stabilise transient ET complexes. We examined the interaction of two components of bacterial photosynthesis, cytochrome c2 and the reaction centre (RC) complex, using dynamic force spectroscopy and PeakForce quantitative nanomechanical imaging. RC–LH1–PufX complexes, attached to silicon nitride AFM probes and maintained in a photo-oxidised state, were lowered onto a silicon oxide substrate bearing dispersed, immobilised and reduced cytochrome c2 molecules. Microscale patterns of cytochrome c2 and the cyan fluorescent protein were used to validate the specificity of recognition between tip-attached RCs and surface-tethered cytochrome c2. Following the transient association of photo-oxidised RC and reduced cytochrome c2 molecules, retraction of the RC-functionalised probe met with resistance, and forces between 112 and 887 pN were required to disrupt the post-ET RC–c2 complex, depending on the retraction velocities used. If tip-attached RCs were reduced instead, the probability of interaction with reduced cytochrome c2 molecules decreased 5-fold. Thus, the redox states of the cytochrome c2 haem cofactor and RC ‘special pair’ bacteriochlorophyll dimer are important for establishing a productive ET complex. The millisecond persistence of the post-ET cytochrome c2[oxidised]–RC[reduced] ‘product’ state is compatible with rates of cyclic photosynthetic ET, at physiologically relevant light intensities.
Biochemical Journal arrow_drop_down http://dx.doi.org/10.1042/BCJ2...Article . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
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For further information contact us at helpdesk@openaire.eumore_vert Biochemical Journal arrow_drop_down http://dx.doi.org/10.1042/BCJ2...Article . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
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For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Journal 2020Publisher:Portland Press Ltd. Funded by:UKRI | Mass spectrometry underpi..., EC | PhotoRedesign, UKRI | Engineering new capacitie...UKRI| Mass spectrometry underpinning synthetic biology, industrial biotechnology and world class bioscience ,EC| PhotoRedesign ,UKRI| Engineering new capacities for solar energy utilisation in bacteriaMatthew P. Johnson; Elizabeth C. Martin; Andrew Hitchcock; Matthew S. Proctor; Jan Pilný; Philip J. Jackson; Marek Pazderník; Marek Pazderník; Roman Sobotka; Roman Sobotka; Mark J. Dickman; C. Neil Hunter; Daniel P. Canniffe;doi: 10.1042/bcj20200561
pmid: 32990304
Chlorophyll synthase (ChlG) catalyses a terminal reaction in the chlorophyll biosynthesis pathway, attachment of phytol or geranylgeraniol to the C17 propionate of chlorophyllide. Cyanobacterial ChlG forms a stable complex with high light-inducible protein D (HliD), a small single-helix protein homologous to the third transmembrane helix of plant light-harvesting complexes (LHCs). The ChlG–HliD assembly binds chlorophyll, β-carotene, zeaxanthin and myxoxanthophyll and associates with the YidC insertase, most likely to facilitate incorporation of chlorophyll into translated photosystem apoproteins. HliD independently coordinates chlorophyll and β-carotene but the role of the xanthophylls, which appear to be exclusive to the core ChlG–HliD assembly, is unclear. Here we generated mutants of Synechocystis sp. PCC 6803 lacking specific combinations of carotenoids or HliD in a background with FLAG- or His-tagged ChlG. Immunoprecipitation experiments and analysis of isolated membranes demonstrate that the absence of zeaxanthin and myxoxanthophyll significantly weakens the interaction between HliD and ChlG. ChlG alone does not bind carotenoids and accumulation of the chlorophyllide substrate in the absence of xanthophylls indicates that activity/stability of the ‘naked’ enzyme is perturbed. In contrast, the interaction of HliD with a second partner, the photosystem II assembly factor Ycf39, is preserved in the absence of xanthophylls. We propose that xanthophylls are required for the stable association of ChlG and HliD, acting as a ‘molecular glue’ at the lateral transmembrane interface between these proteins; roles for zeaxanthin and myxoxanthophyll in ChlG–HliD complexation are discussed, as well as the possible presence of similar complexes between LHC-like proteins and chlorophyll biosynthesis enzymes in plants.
CORE arrow_drop_down add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1042/bcj20200561&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert CORE arrow_drop_down add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
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For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Journal 2022 United KingdomPublisher:Elsevier BV Funded by:UKRI | Sheffield antimicrobial r..., UKRI | Engineering new capacitie..., UKRI | Elucidating the transient... +2 projectsUKRI| Sheffield antimicrobial resistance network - SHAMROK ,UKRI| Engineering new capacities for solar energy utilisation in bacteria ,UKRI| Elucidating the transient nature of electron transfer complexes at the single-molecule level ,UKRI| Quantification of the forces that mediate electron transfers between proteins ,EC| PhotoRedesignVasilev, C.; Swainsbury, D.J.K.; Cartron, M.L.; Martin, E.C.; Kumar, S.; Hobbs, J.K.; Johnson, M.P.; Hitchcock, A.; Hunter, C.N.;pmid: 34793767
In the model purple phototrophic bacterium Rhodobacter (Rba.) sphaeroides, solar energy is converted via coupled electron and proton transfer reactions within the intracytoplasmic membranes (ICMs), infoldings of the cytoplasmic membrane that form spherical 'chromatophore' vesicles. These bacterial 'organelles' are ideal model systems for studying how the organisation of the photosynthetic complexes therein shape membrane architecture. In Rba. sphaeroides, light-harvesting 2 (LH2) complexes transfer absorbed excitation energy to dimeric reaction centre (RC)-LH1-PufX complexes. The PufX polypeptide creates a channel that allows the lipid soluble electron carrier quinol, produced by RC photochemistry, to diffuse to the cytochrome bc1 complex, where quinols are oxidised to quinones, with the liberated protons used to generate a transmembrane proton gradient and the electrons returned to the RC via cytochrome c2. Proximity between cytochrome bc1 and RC-LH1-PufX minimises quinone/quinol/cytochrome c2 diffusion distances within this protein-crowded membrane, however this distance has not yet been measured. Here, we tag the RC and cytochrome bc1 with yellow or cyan fluorescent proteins (YFP/CFP) and record the lifetimes of YFP/CFP Förster resonance energy transfer (FRET) pairs in whole cells. FRET analysis shows that that these complexes lie on average within 6 nm of each other. Complementary high-resolution atomic force microscopy (AFM) of intact, purified chromatophores verifies the close association of cytochrome bc1 complexes with RC-LH1-PufX dimers. Our results provide a structural basis for the close kinetic coupling between RC-LH1-PufX and cytochrome bc1 observed by spectroscopy, and explain how quinols/quinones and cytochrome c2 shuttle on a millisecond timescale between these complexes, sustaining efficient photosynthetic electron flow.
CORE arrow_drop_down CORE (RIOXX-UK Aggregator)Article . 2022License: CC BY NC NDData sources: CORE (RIOXX-UK Aggregator)Biochimica et Biophysica Acta (BBA) - BioenergeticsArticle . 2022 . Peer-reviewedLicense: Elsevier Non-CommercialData sources: CrossrefBiochimica et Biophysica ActaArticle . 2022 . Peer-reviewedData sources: European Union Open Data PortalUniversity of East Anglia: UEA Digital RepositoryArticle . 2022Data sources: Bielefeld Academic Search Engine (BASE)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1016/j.bbabio.2021.148508&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert CORE arrow_drop_down CORE (RIOXX-UK Aggregator)Article . 2022License: CC BY NC NDData sources: CORE (RIOXX-UK Aggregator)Biochimica et Biophysica Acta (BBA) - BioenergeticsArticle . 2022 . Peer-reviewedLicense: Elsevier Non-CommercialData sources: CrossrefBiochimica et Biophysica ActaArticle . 2022 . Peer-reviewedData sources: European Union Open Data PortalUniversity of East Anglia: UEA Digital RepositoryArticle . 2022Data sources: Bielefeld Academic Search Engine (BASE)add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1016/j.bbabio.2021.148508&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Journal 2019 United KingdomPublisher:Oxford University Press (OUP) Funded by:UKRI | Engineering new capacitie...UKRI| Engineering new capacities for solar energy utilisation in bacteriaWilliam H.J. Wood; Samuel F.H. Barnett; Sarah Flannery; C. Neil Hunter; Matthew P. Johnson;doi: 10.1104/pp.19.00503
Grana stacking in plant chloroplast thylakoid membranes dynamically responds to the light environment. These dynamics have been linked to regulation of the relative antenna sizes of PSI and PSII (state transitions), the PSII repair cycle, and the regulation of photosynthetic electron transfer. Here, we used 3D structured illumination microscopy, a subdiffraction-resolution fluorescence imaging technique, to investigate the light-intensity dependence, kinetics, reversibility, and regulation of dynamic thylakoid stacking in spinach (Spinacia oleracea) and Arabidopsis (Arabidopsis thaliana). Low-intensity white light (150 μmol photons m−2 s−1) behaved similarly to light preferentially exciting PSII (660 nm), causing a reduction in grana diameter and an increased number of grana per chloroplast. By contrast, high-intensity white light (1000 μmol photons m−2 s−1), darkness, and light preferentially exciting PSI (730 nm) reversed these changes. These dynamics occurred with a half-time of 7 to 8 min and were accompanied by state transitions. Consistent with this, the dynamics were dependent on STN7 (light-harvesting complex II [LHCII] kinase) and TAP38 (LHCII phosphatase), which are required for state transitions but were unaffected by the absence of STN8 (PSII kinase) or PSII core phosphatase (PSII phosphatase). Unlike state transitions, however, thylakoid stacking dynamics did not rely on the presence of the LHCI and PSI subunit L phospho-LHCII binding sites on PSI. Since oligomerization of thylakoid curvature protein (CURT1A) was unaffected by the absence of STN7 or TAP38, we conclude that the primary determinant of dynamic thylakoid stacking is LHCII phosphorylation.
PLANT PHYSIOLOGY arrow_drop_down add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
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You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1104/pp.19.00503&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eumore_vert PLANT PHYSIOLOGY arrow_drop_down add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1104/pp.19.00503&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Other literature type , Journal 2019 United KingdomPublisher:Springer Science and Business Media LLC Funded by:UKRI | Engineering new capacitie..., UKRI | Quantification of the for..., NIH | Center for Macromolecular... +3 projectsUKRI| Engineering new capacities for solar energy utilisation in bacteria ,UKRI| Quantification of the forces that mediate electron transfers between proteins ,NIH| Center for Macromolecular Modeling and Bioinformatics ,UKRI| Mass spectrometry underpinning synthetic biology, industrial biotechnology and world class bioscience ,EC| SYNTHPHOTO ,UKRI| Revealing a mechanistic understanding of the role of viruses and host nutrient status in modulating CO2 fixation in key marine phototrophsC. MacGregor-Chatwin; P. J. Jackson; M. Sener; J. W. Chidgey; A. Hitchcock; P. Qian; G. E. Mayneord; M. P. Johnson; Z. Luthey-Schulten; M. J. Dickman; D. J. Scanlan; C. N. Hunter;Prochlorococcus is a major contributor to primary production, and globally the most abundant photosynthetic genus of picocyanobacteria because it can adapt to highly stratified low-nutrient conditions that are characteristic of the surface ocean. Here, we examine the structural adaptations of the photosynthetic thylakoid membrane that enable different Prochlorococcus ecotypes to occupy high-light, low-light and nutrient-poor ecological niches. We used atomic force microscopy to image the different photosystem I (PSI) membrane architectures of the MED4 (high-light) Prochlorococcus ecotype grown under high-light and low-light conditions in addition to the MIT9313 (low-light) and SS120 (low-light) Prochlorococcus ecotypes grown under low-light conditions. Mass spectrometry quantified the relative abundance of PSI, photosystem II (PSII) and cytochrome b6f complexes and the various Pcb proteins in the thylakoid membrane. Atomic force microscopy topographs and structural modelling revealed a series of specialized PSI configurations, each adapted to the environmental niche occupied by a particular ecotype. MED4 PSI domains were loosely packed in the thylakoid membrane, whereas PSI in the low-light MIT9313 is organized into a tightly packed pseudo-hexagonal lattice that maximizes harvesting and trapping of light. There are approximately equal levels of PSI and PSII in MED4 and MIT9313, but nearly twofold more PSII than PSI in SS120, which also has a lower content of cytochrome b6f complexes. SS120 has a different tactic to cope with low-light levels, and SS120 thylakoids contained hundreds of closely packed Pcb-PSI supercomplexes that economize on the extra iron and nitrogen required to assemble PSI-only domains. Thus, the abundance and widespread distribution of Prochlorococcus reflect the strategies that various ecotypes employ for adapting to limitations in light and nutrient levels.
CORE arrow_drop_down http://dx.doi.org/10.1038/s414...Article . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
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For further information contact us at helpdesk@openaire.eumore_vert CORE arrow_drop_down http://dx.doi.org/10.1038/s414...Article . Peer-reviewedData sources: European Union Open Data Portaladd ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
You have already added works in your ORCID record related to the merged Research product.All Research productsarrow_drop_down <script type="text/javascript"> <!-- document.write('<div id="oa_widget"></div>'); document.write('<script type="text/javascript" src="https://beta.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=10.1038/s41477-019-0475-z&type=result"></script>'); --> </script>
For further information contact us at helpdesk@openaire.eudescription Publicationkeyboard_double_arrow_right Article , Other literature type , Journal 2020Publisher:Wiley Funded by:UKRI | Mass spectrometry underpi..., UKRI | SHeffield IMAging (SHIMA), UKRI | Engineering new capacitie...UKRI| Mass spectrometry underpinning synthetic biology, industrial biotechnology and world class bioscience ,UKRI| SHeffield IMAging (SHIMA) ,UKRI| Engineering new capacities for solar energy utilisation in bacteriaAuthors: Sarah E. Flannery; Christopher Hepworth; William H. J. Wood; Federica Pastorelli; +4 AuthorsSarah E. Flannery; Christopher Hepworth; William H. J. Wood; Federica Pastorelli; Christopher N. Hunter; Mark J. Dickman; Philip J. Jackson; Matthew P. Johnson;SummaryPhotosynthetic acclimation, the ability to adjust the composition of the thylakoid membrane to optimise the efficiency of electron transfer to the prevailing light conditions, is crucial to plant fitness in the field. While much is known about photosynthetic acclimation in Arabidopsis, to date there has been no study that combines both quantitative label‐free proteomics and photosynthetic analysis by gas exchange, chlorophyll fluorescence and P700 absorption spectroscopy. Using these methods we investigated how the levels of 402 thylakoid proteins, including many regulatory proteins not previously quantified, varied upon long‐term (weeks) acclimation of Arabidopsis to low (LL), moderate (ML) and high (HL) growth light intensity and correlated these with key photosynthetic parameters. We show that changes in the relative abundance of cytb6f, ATP synthase, FNR2, TIC62 and PGR6 positively correlate with changes in estimated PSII electron transfer rate and CO2 assimilation. Improved photosynthetic capacity in HL grown plants is paralleled by increased cyclic electron transport, which positively correlated with NDH, PGRL1, FNR1, FNR2 and TIC62, although not PGR5 abundance. The photoprotective acclimation strategy was also contrasting, with LL plants favouring slowly reversible non‐photochemical quenching (qI), which positively correlated with LCNP, while HL plants favoured rapidly reversible quenching (qE), which positively correlated with PSBS. The long‐term adjustment of thylakoid membrane grana diameter positively correlated with LHCII levels, while grana stacking negatively correlated with CURT1 and RIQ protein abundance. The data provide insights into how Arabidopsis tunes photosynthetic electron transfer and its regulation during developmental acclimation to light intensity.
add ClaimPlease grant OpenAIRE to access and update your ORCID works.This Research product is the result of merged Research products in OpenAIRE.
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You have already added works in your ORCID record related to the merged Research product.This Research product is the result of merged Research products in OpenAIRE.
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