《植物生理学报》 2013, 49(8): 715-721

植物中的蛋白质二硫键异构酶及其类蛋白

陈珍¹, 江琼², 朱诚^2,*

1台州学院生命科学学院, 浙江台州318000; 2中国计量学院生命科学学院, 杭州310018

通信作者：朱诚；E-mail: pzhch@cjlu.edu.cn；Tel: 0571-86914510

摘　要：

摘要: 蛋白质二硫键异构酶(protein disulfide isomerase, PDI)及其类蛋白, 是硫氧还蛋白超家族的一员, 具有催化蛋白质二硫键氧化、还原和异构的功能, 并具有分子伴侣和抗分子伴侣活性及钙离子结合位点, 在生物体内起着极其重要的作用。本文综述了近年来对植物PDILs的相关了解, 总结了PDI类蛋白的结构、表达、定位、生化与生物学功能, 也结合本实验室的工作, 对水稻等PDI的相关信息与作用做了简要阐述, 为加快这一重要酶及分子伴侣的研究提供启示。

关键词：蛋白质二硫键异构酶; 分子伴侣; 二硫键氧化与还原; 二硫键异构

收稿：2013-05-08   修定：2013-07-01

资助：浙江省自然科学基金(Y3110362)

Protein Disulfide Isomerise and PDI-Like Proteins in Plant

CHEN Zhen¹, JIANG Qiong², ZHU Cheng^2,*

¹College of Life Sciences, Taizhou University, Taizhou, Zhejiang 318000, China; ²College of Life Sciences, China Jiliang University, Hangzhou 310018, China

Corresponding author: ZHU Cheng; E-mail: pzhch@cjlu.edu.cn; Tel: 0571-86914510

Abstract:

Protein disulfide isomerase (PDI) and PDI-like proteins (PDILs), belonging to thioredoxin (Trx) su-perfamily, have diverse functions in organisms. They can catalyze thiol-disulfide interchange, resulting in the formation, reduction, or isomerization of protein disulfide bonds in protein substrates. They also display chaper-one activity and anti-chaperone activity. Furthermore, they have Ca2+-binding domain. Researches about PDI and PDILs from plant were summarized in this paper, including structure, expression, location, chemical func-tion and biological role. Related work by our research group about PDILs in rice was also presented. It may bring us a good insight for further research about this enzyme or chaperone with important roles.

Key words: protein disulfide isomerase; chaperone; oxidation or reduction of disulfide bonds; isomerization of disulfide bonds