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论文摘要

拟南芥 BAH1 与大肠杆菌热胁迫耐受的关系分析

Functional analysis of Arabidopsis thaliana BAH1 in

作者:梁可(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; 河南科技大学医学院);牛毓龙(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:LIANG Ke(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; Medical College, Henan Science and Technology University);NIU Yu-Long(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:2016-01-08          年卷(期)页码:2017,54(3):623-628

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:锌指;BAH1;DnaJ;E3泛素连接酶

Key words:zinc finger; BAH1; DnaJ; ubiquitin E3 ligase

基金项目:国家高技术研究发展计划,863计划(2012AA022204)

中文摘要

泛素化是生物体内重要的蛋白修饰途径,E3泛素连接酶具有底物蛋白的特异识别功能。拟南芥BAH1含有保守的C3H4型RING结构域,能结合两个锌离子形成交叉式锌指结构,与DnaJ锌指结构类似。通过体外泛素化实验证明BAH1具有E3连接酶活性。在大肠杆菌(E. coli)中的热敏感表型弥补实验发现BAH1具有DnaJ锌指结构类似的功能。因此,BAH1在E. coli中的功能有可能与DnaJ相似,通过锌指结构参与DnaK/DnaJ伴侣系统发挥功能。

英文摘要

Protein ubiquitination is one classic type of post-translational modification. The ubiquitin ligase E3 could interact directly with the substrate and mediate in large part the ubiquitination specificity. Arabidopsis thaliana BAH1 encodes a ubiquitin E3 ligase with a C3HC4-RING finger domain, which could bind two zinc ions to form a cross brace zinc finger. Here, we found the zinc finger structure of BAH1 and DnaJ was similar. Further self-ubiquitination assay in vitro demonstrated BAH1 possessed E3 ligase activity. We also found BAH1 can confer heat tolerance of E. coli as DnaJ by temperature-sensitive assays. Hence, these results indicated that BAH1 may improve heat tolerance of E. coli through interacting with DnaK/DnaJ chaperone system.

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