FEBS Letters | |
Arabidopsis glutathione‐dependent formaldehyde dehydrogenase is an S‐nitrosoglutathione reductase | |
Sakamoto, Atsushi2  Morikawa, Hiromichi2  Ueda, Manami1  | |
[1] Department of Curriculum and Instruction, Faculty of Education, Hiroshima University, 1-1-2 Kagamiyama, Higashi-Hiroshima 739-8523, Japan;Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, 1-3-1 Kagamiyama, Higashi-Hiroshima 739-8526, Japan | |
关键词: Glutathione-dependent formaldehyde dehydrogenase; S–Nitrosoglutathione reductase; Nitrosative stress; Nitric oxide signaling; Arabidopsis; GS-FDH; glutathione-dependent formaldehyde dehydrogenase; GSNO; S-nitrosoglutathione; GSNOR; GSNO reductase; IPTG; isopropyl 1-thio-β-D-galactoside; NO; nitric oxide; PCR; polymerase chain reaction; RNI; reactive nitrogen intermediate; SDS–PAGE; sodium dodecyl sulfate–polyacrylamide gel electrophoresis; SNO; S-nitrosothiol; | |
DOI : 10.1016/S0014-5793(02)02414-6 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020311604ZK.pdf | 117KB | download |