期刊
PLANT SCIENCE
卷 185, 期 -, 页码 86-96出版社
ELSEVIER IRELAND LTD
DOI: 10.1016/j.plantsci.2012.01.005
关键词
Thiol-based redox regulation; Glutaredoxin; Glutathione; Reactive oxygen species; Redox signaling
资金
- Ministero dell'Istruzione, dell'Universita e della Ricerca of Italy
- ANR [08-BLAN-0153 GLUTAPHOTO]
Reactive oxygen species play important roles in redox signaling mainly through a set of reversible post-translational modifications of cysteine thiol residues in proteins, including glutathionylation and dithiol/disulfide exchange. Protein glutathionylation has been extensively studied in mammals but emerging evidence suggests that it can play important roles in plants and in chloroplast in particular. This redox modification involves protein thiols and glutathione and is mainly controlled by glutaredoxins, oxidoreductases belonging to the thioredoxin superfamily. In this review, we first present the possible mechanisms of protein glutathionylation and then introduce the chloroplast systems of glutaredoxins and thioredoxins, in order to pinpoint the biochemical properties that make some glutaredoxin isoforms the master enzymes in deglutathionylation. Finally, we discuss the possible roles of glutathionylation in thiol protection, protein regulation, reactive oxygen species scavenging and redox signaling in chloroplasts, with emphasis on the crosstalk between thioredoxin- and glutaredoxin-mediated signaling pathways. (C) 2012 Elsevier Ireland Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据