Expression of Bacterial l-aspartate-α-decarboxylase in Tobacco Increases β-Alanine and Pantothenate Levels and Improves Thermotolerance
Copyright policy )Expression of Bacterial l-aspartate-α-decarboxylase in Tobacco Increases β-Alanine and Pantothenate Levels and Improves Thermotolerance
L- Aspartate-alpha-decarboxylase catalyzes the decarboxylation of L -aspartate to generate Beta-alanine and carbon dioxide. This is an unusual pyruvoyl-dependent enzyme unique to prokaryotes that undergoes limited self-processing. The Escherichia coli pan D gene encoding L- aspartate-alpha-decarboxylase was expressed under a constitutive promoter in transgenic tobacco. Transgene expression was verified by assays based on RNA blots, immunoblots and enzyme activity in vitro. The pan D lines had increased levels of leaf Beta-alanine (1.2- to 4-fold), pantothenate (3.2- to 4.1-fold) and total free amino acids (up to 3.7-fold) compared to wild-type and vector controls. Growth of homozygous lines expressing E. coli L- aspartate-alpha-decarboxylase was less affected than that of the control lines when the plants were stressed for 1 week at 35 degrees C. When transferred from 35 to 30 degrees C for 3 weeks, the Pan D transgenic lines recovered significantly (P
- Florida Southern College United States
Nicotiana, Glutamate Decarboxylase, Acclimatization, Temperature, Gene Expression, Germination, Plants, Genetically Modified, Pantothenic Acid, Plant Leaves, Phenotype, Genes, Bacterial, Seeds, Escherichia coli, beta-Alanine, Biomass, RNA, Messenger
Nicotiana, Glutamate Decarboxylase, Acclimatization, Temperature, Gene Expression, Germination, Plants, Genetically Modified, Pantothenic Acid, Plant Leaves, Phenotype, Genes, Bacterial, Seeds, Escherichia coli, beta-Alanine, Biomass, RNA, Messenger
