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论文题目: Characterization of the oxidative protein folding activity of a unique plant oxidoreductase, Arabidopsis protein disulfide isomerase-11
论文编号:
作者: Fan Fenggui(范锋贵), Yini Zhang, Wang Shen(王珅), Han Yongfeng (韩永峰),Wang Lei *, Lu Dongping*(吕东平)
刊物名称: Biochemical and Biophysical Research Communications
卷期页码: Online, ,
发表年度: 2017
DOI: https://doi.org/10.1016/j.bbrc.2017.11.111
摘要:

 

Protein disulfide isomerases (PDIs) can catalyze disulfide bond formation in nascent secretory proteins and membrane proteins and can introduce correct disulfide bonds into substrate proteins containing mispaired disulfides. The functions of mammalian PDIs have been extensively studied; however, relative to mammalian PDIs, the systematic characterization of PDIs for their oxidoreductase activity in plants is still lacking. Arabidopsis protein disulfide isomerases-11 (AtPDI11), with the structure of a-a'-D, has no ortholog in animals or yeast. In this study, we demonstrated that AtPDI11 has oxidoreductase activity in vitro using a GSSG/GSH-mediated oxidative protein folding system. Moreover, the active site in the a' domain of AtPDI11 is critical for its oxidative folding activity. AtPDI11 is present in four redox forms in vivo, which are determined by the active site cysteines (Cys52 and Cys55 in the a domain, and Cys171 and Cys174 in the a' domain). Genetic evidence suggests that AtPDI11 is required for plant growth under reducing conditions. Our work provides an example for studying the oxidoreductase function of other plant PDIs.

 

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