Abstract
S-Nitrosoglutathione (GSNO), an adduct of nitric oxide (NO) with glutathione, is known as a biological NO reservoir. Heterologous expression in Escherichia coli of a cDNA encoding a glutathione-dependent formaldehyde dehydrogenase of Arabidopsis thaliana showed that the recombinant protein reduces GSNO. The identity of the cDNA was further confirmed by functional complementation of the hypersensitivity to GSNO of a yeast mutant with impaired GSNO metabolism. This is the first demonstration of a plant GSNO reductase, suggesting that plants possess the enzymatic pathway that modulates the bioactivity and toxicity of NO.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aldehyde Oxidoreductases / genetics
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Aldehyde Oxidoreductases / metabolism*
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Arabidopsis / enzymology*
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Cloning, Molecular
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DNA, Complementary / genetics
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DNA, Complementary / metabolism
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Escherichia coli / metabolism
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Gene Expression
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Genetic Complementation Test
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Oxidation-Reduction
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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S-Nitrosoglutathione / metabolism*
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S-Nitrosoglutathione / pharmacology
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Saccharomyces / drug effects
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Saccharomyces / genetics
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Saccharomyces / metabolism
Substances
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DNA, Complementary
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Recombinant Proteins
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S-Nitrosoglutathione
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formaldehyde dehydrogenase (glutathione)
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Aldehyde Oxidoreductases