Thiol-disulfide exchange between the PDI family of oxidoreductases negates the requirement for an oxidase or reductase for each enzyme

被引:36
作者
Oka, Ojore B. V. [1 ]
Yeoh, Hui Y. [1 ]
Bulleid, Neil J. [1 ]
机构
[1] Univ Glasgow, Inst Mol Cell & Syst Biol, CMVLS, Glasgow G12 8QQ, Lanark, Scotland
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
disulfide formation; electron transfer; endoplasmic reticulum; protein disulfide isomerase; redox potential; thiol-disulfide exchange; ENDOPLASMIC-RETICULUM; ESCHERICHIA-COLI; BOND FORMATION; HUMAN PROTEIN; ELECTRON-TRANSFER; STRUCTURAL BASIS; REDOX; ER; OXIDATION; PEROXIREDOXIN;
D O I
10.1042/BJ20141423
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
The formation of disulfides in proteins entering the secretory pathway is catalysed by the protein disulfide isomerase (PDI) family of enzymes. These enzymes catalyse the introduction, reduction and isomerization of disulfides. To function continuously they require an oxidase to reform the disulfide at their active site. To determine how each family member can be recycled to catalyse disulfide exchange, we have studied whether disulfides are transferred between individual PDI family members. We studied disulfide exchange either between purified proteins or by identifying mixed disulfide formation within cells grown in culture. We show that disulfide exchange occurs efficiently and reversibly between specific PDIs. These results have allowed us to define a hierarchy for members of the PDI family, in terms of ability to act as electron acceptors or donors during thiol-disulfide exchange reactions and indicate that there is no kinetic barrier to the exchange of disulfides between several PDI proteins. Such promiscuous disulfide exchange negates the necessity for each enzyme to be oxidized by Ero1 (ER oxidoreductin 1) or reduced by a reductive system. The lack of kinetic separation of the oxidative and reductive pathways in mammalian cells contrasts sharply with the equivalent systems for native disulfide formation within the bacterial periplasm.
引用
收藏
页码:279 / 288
页数:10
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