Monothiol glutaredoxins: a common domain for multiple functions

被引:181
作者
Herrero, E. [1 ]
de la Torre-Ruiz, M. A. [1 ]
机构
[1] Univ Lleida, IRBLLEIDA, Dept Ciencies Med Basiques, Lleida 25008, Spain
关键词
glutaredoxin; redox regulation; glutathione; oxidative stress; iron-sulfur cluster; transcription regulator; signal transduction;
D O I
10.1007/s00018-007-6554-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Monothiol glutaredoxins with the CGFS sequence at the active site are widespread among prokaryotes and eukaryotes. Two subclasses exist, those with a single glutaredoxin domain and those with a thioredoxin-like region followed by one or more glutaredoxin domains. Studies in Saccharomyces cerevisiae have demonstrated the role of the Grx5 protein in the biogenesis of iron-sulfur clusters. Grx5 homologues in other eukaryotes could carry out similar functions. Two S. cerevisiae monothiol glutaredoxins with the thioredoxin-like extension, Grx3 and Grx4, are modulators of the transcriptional activator Aft1, which regulates iron uptake in yeast. The human PICOT protein is a Grx3/Grx4 homologue with the same hybrid primary structure that regulates protein kinase C activity and may participate in physiological processes such as control of cardiac function. Therefore, monothiol glutaredoxins share a common basic structural motif and biochemical mechanism of action, while participating in a diversity of cellular functions as protein redox regulators.
引用
收藏
页码:1518 / 1530
页数:13
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