| 拟南芥 BAH1 与大肠杆菌热胁迫耐受的关系分析 |
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| 引用本文： | 梁可,徐西兵,牛毓龙,杨毅.拟南芥 BAH1 与大肠杆菌热胁迫耐受的关系分析[J].四川大学学报(自然科学版),2017,54(3):623-628. |
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| 作者姓名： | 梁可 徐西兵 牛毓龙 杨毅 |
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| 作者单位： | 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,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,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, |
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| 基金项目： | 国家高技术研究发展计划,863计划（2012AA022204） |
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| 摘 要： | 拟南芥BAH1含有保守的C3H4型RING结构域,与DnaJ锌指结构类似.利用原核表达纯化的BAH1进行体外泛素化实验证明了BAH1具有E3连接酶活性.然后通过表型回复实验发现BAH1融合J-domain结构域后(JdBAH1)和DnaJ一样能明显弥补danJ突变株MF634的热敏表型,在43℃存活;而转入突变锌指结构的JdBAH1C231S,C234S,C276S,C279S(JdBAH1△Zn1/2)菌株在43℃高温条件下不能存活,说明BAH1在大肠杆菌内具有类似DnaJ锌指结构的功能.因此,BAH1在E.coli中的功能有可能与DnaJ相似,通过锌指结构参与了DnaK/DnaJ伴侣系统发挥功能.
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| 关 键 词： | 锌指 BAH1 DnaJ E3泛素连接酶 |
| 收稿时间： | 2016/1/8 0:00:00 |
| 修稿时间： | 2016/4/9 0:00:00 |
Functional analysis of Arabidopsis thaliana BAH1 in |
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| LIANG Ke,XU Xi-Bing,NIU Yu-Long and YANG Yi.Functional analysis of Arabidopsis thaliana BAH1 in[J].Journal of Sichuan University (Natural Science Edition),2017,54(3):623-628. |
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| Authors: | LIANG Ke XU Xi-Bing NIU Yu-Long and YANG Yi |
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| Institution: | Key Laboratory of Bio-resources and Eco-environment of Ministry of Education, College of Life Sciences, Sichuan University,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,Key Laboratory of Bio-resources and Eco-environment of Ministry of Education, College of Life Sciences, Sichuan University and Key Laboratory of Bio-resources and Eco-environment of Ministry of Education, College of Life Sciences, Sichuan University |
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| Abstract: | 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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| Keywords: | zinc finger BAH1 DnaJ ubiquitin E3 ligase |
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