拟南芥Hsp40蛋白AtDjA5在大肠杆菌中的功能分析
Functional analysis of the Arabidopsis thaliana Hsp40 protein AtDjA5 in Escherichia coli
作者：陈 鹏(四川大学生命科学学院生物资源与生态环境教育部重点实验室)；徐西兵(四川大学生命科学学院生物资源与生态环境教育部重点实验室)；胡屹玲(四川大学生命科学学院生物资源与生态环境教育部重点实验室)；杨 毅(四川大学生命科学学院生物资源与生态环境教育部重点实验室)
Author：CHEN Peng(Key laboratory of Bio resources and Eco environment of Ministry of Education,College of Life Sciences, Sichuan University)；XU Xi Bing(Key laboratory of Bio resources and Eco environment of Ministry of Education,College of Life Sciences, Sichuan University)；HU Yi Ling(Key laboratory of Bio resources and Eco environment of Ministry of Education,College of Life Sciences, Sichuan University)；YANG Yi(Key laboratory of Bio resources and Eco environment of Ministry of Education,College of Life Sciences, Sichuan University)
收稿日期：2014-02-21 年卷（期）页码：2015,52(5):1117-1122
期刊名称：四川大学学报: 自然科学版
Journal Name：Journal of Sichuan University (Natural Science Edition)
关键字：热激蛋白; Hsp40; DnaJ; AtDjA5; 免疫共沉淀; Western blot
Key words：Heat shock protein; Hsp40; DnaJ; AtDjA5; Co immunoprecipitation; Western blot
基金项目：国家863项目（2012AA022204）， 国家自然科学基金（31171586）
中文摘要
通过分析大肠杆菌dnaJ缺失菌株在43℃下的生长表型, 发现AtDjA5及其J Domain能够功能性地替换DnaJ及其J Domain. 免疫共沉淀实验结果表明AtDjA5与DnaK存在相互作用. 由Western blot检测推测AtDjA5能够稳定大肠杆菌热激转录因子σ32并下调热激蛋白DnaK表达量. 这些发现说明AtDjA5在大肠杆菌中具有与DnaJ相似的功能.
英文摘要
By analyzing growth phenotype of the dnaJ mutant strain at 43℃, AtDjA5 and its J Domain can functionally substitute for DnaJ and its J Domain. Co immunoprecipitation experiments show that AtDjA5 can interact with DnaK. It’s speculated that AtDjA5 can stabilize the heat shock factor σ32 of E. coli and down regulate the expression of Dnak by western blot analysis. These findings suggest that AtDjA5 has a similar function with DnaJ in E. coli.
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