Gene expression of ascorbic acid-related enzymes in tobacco

GDP- d-mannose pyrophosphorylase (GMPase) and l-galactono-1, 4-lactone dehydrogenase (GalLDH) are key enzymes in l-ascorbic acid (AsA) biosynthesis of plants, and a full-length cDNA for GMPase was isolated from tobacco using PCR. Additionally, expression of GMPase, GalLDH and other AsA-related enzym...

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Bibliographic Details
Published in:Phytochemistry (Oxford) 2002-11, Vol.61 (6), p.631-635
Main Authors: Tabata, Kazufumi, Takaoka, Takahiko, Esaka, Muneharu
Format: Article
Language:English
Subjects:
Ascorbate oxidase
Ascorbate peroxidase
Ascorbic acid
Ascorbic Acid - metabolism
Base Sequence
Biological and medical sciences
Blotting, Northern
DNA Primers
DNA, Complementary
Fundamental and applied biological sciences. Psychology
GDP- d-Mannose pyrophosphorylase
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Plant
l-Galactono-1,4-lactone dehydrogenase
Metabolism
Metabolism. Physicochemical requirements
Nicotiana - genetics
Nucleotidyltransferases - genetics
Oxidoreductases - genetics
Oxidoreductases Acting on CH-CH Group Donors
Plant physiology and development
RNA, Messenger - genetics
Solanaceae
Tobacco ( Nicotiana tabacum L.)
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Summary:GDP- d-mannose pyrophosphorylase (GMPase) and l-galactono-1, 4-lactone dehydrogenase (GalLDH) are key enzymes in l-ascorbic acid (AsA) biosynthesis of plants, and a full-length cDNA for GMPase was isolated from tobacco using PCR. Additionally, expression of GMPase, GalLDH and other AsA-related enzymes was examined in tobacco tissues and cultured BY-2 cells, and the relationship between their expression patterns and AsA content is discussed. It was found that the expression of GalLDH and GMPase mRNAs was markedly suppressed by loading AsA, suggesting that AsA concentration in the cells may regulate AsA biosynthesis. Moreover, the expression of GMPase and GalLDH mRNAs in tobacco leaf also suggested that AsA biosynthesis may be induced by light. Ascorbic acid content and gene expression of ascorbic acid-related enzymes were investigated in tobacco BY-2 cells.
ISSN:0031-9422
1873-3700
DOI:10.1016/S0031-9422(02)00367-9