Protein S-thiolation by glutathionylspermidine (Gsp): The role of Escherichia coli Gsp synthetase/amidase in redox regulation

Bing Yu Chiang, Tzu Chieh Chen, Chien Hua Pai, Chi Chi Chou, Hsuan He Chen, Tzu Ping Ko, Wen Hung Hsu, Chun Yang Chang, Whei Fen Wu, Andrew H.J. Wang, Chun Hung Lin

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31 引文 斯高帕斯(Scopus)

摘要

Certain bacteria synthesize glutathionylspermidine (Gsp), from GSH and spermidine. Escherichia coli Gsp synthetase/amidase (GspSA) catalyzes both the synthesis and hydrolysis of Gsp. Prior to the work reported herein, the physiological role(s) of Gsp or how the two opposing GspSA activities are regulated had not been elucidated. We report that Gsp-modified proteins from E. coli contain mixed disulfides of Gsp and protein thiols, representing a new type of post-translational modification formerly undocumented. The level of these proteins is increased by oxidative stress. We attribute the accumulation of such proteins to the selective inactivation of GspSA amidase activity. X-ray crystallography and a chemical modification study indicated that the catalytic cysteine thiol of the GspSA amidase domain is transiently inactivated byH 2O2 oxidation to sulfenic acid, which is stabilized by a very short hydrogen bond with a water molecule. We propose a set of reactions that explains how the levels of Gsp and Gsp S-thiolated proteins are modulated in response to oxidative stress. The hypersensitivities of GspSA and GspSA/glutaredoxin null mutants toH2O2 support the idea that GspSA and glutaredoxin act synergistically to regulate the redox environment of E. coli.

原文英語
頁(從 - 到)25345-25353
頁數9
期刊Journal of Biological Chemistry
285
發行號33
DOIs
出版狀態已發佈 - 8月 13 2010
對外發佈

ASJC Scopus subject areas

  • 生物化學
  • 分子生物學
  • 細胞生物學

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