Expression of Bacterial l-aspartate-α-decarboxylase in Tobacco Increases β-Alanine and Pantothenate Levels and Improves Thermotolerance View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-03

AUTHORS

Walid M. Fouad, Bala Rathinasabapathi

ABSTRACT

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 More... »

PAGES

495-505

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s11103-005-4844-9

DOI

http://dx.doi.org/10.1007/s11103-005-4844-9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046618376

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16525887


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