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学科主题: 基础医学
题名:
Crystal structure and function of an unusual dimeric Hsp20.1 provide insight into the thermal protection mechanism of small heat shock proteins
作者: Liu, Liang1; Chen, Jiyun2,3; Yang, Bo1; Wang, Yonghua4
关键词: Small heat shock protein (sHSP) ; Crystal structure ; Dimerization ; Chaperone activity
刊名: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
发表日期: 2015-03-06
DOI: 10.1016/j.bbrc.2015.01.134
卷: 458, 期:2, 页:429-434
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemistry & Molecular Biology ; Biophysics
研究领域[WOS]: Biochemistry & Molecular Biology ; Biophysics
关键词[WOS]: ALPHA-B-CRYSTALLIN ; N-TERMINAL REGION ; CHAPERONE ACTIVITY ; BINDING ; DOMAIN ; STHSP14.0 ; HSP16.5 ; STRESS ; MOTIF
英文摘要:

Small heat shock proteins (sHSPs) are ubiquitous chaperones that play a vital role in protein homeostasis. sHSPs are characterized by oligomeric architectures and dynamic exchange of subunits. The flexible oligomeric assembling associating with function remains poorly understood. Based on the structural data, it is certainly agreed that two dimerization models depend on the presence or absence of a 06 strand to differentiate nonmetazoan sHSPs from metazoan sHSPs. Here, we report the Sulfolobus solfataricus Hsp20.1 ACD dimer structure, which shows a distinct dimeric interface. We observed that, in the absence of beta 6, Hsp20.1 dimer does not depend on beta 7 strand for forming dimer interface as metazoan sHSPs, nor dissociates to monomers. This is in contrast to other published sHSPs. Our structure reveals a variable, highly polar dimer interface that has advantages for rapid subunits exchange and substrate binding. Remarkably, we find that the C-terminal truncation variant has chaperone activity comparable to that of wild-type despite lack of the oligomer structure. Our further study indicates that the N-terminal region is essential for the oligomer and dimer binding to the target protein. Together, the structure and function of Hsp20.1 give more insight into the thermal protection mechanism of sHSPs. (C) 2015 Elsevier Inc. All rights reserved.

语种: 英语
所属项目编号: 2014ZM0062 ; S2012040007734
项目资助者: Fundamental Research Funds for the Central Universities ; PhD Start-up Fund of Natural Science Foundation of Guangdong Province
WOS记录号: WOS:000351482200035
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.bjmu.edu.cn/handle/400002259/59934
Appears in Collections:基础医学院_北京大学系统生物医学研究所_期刊论文

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作者单位: 1.S China Univ Technol, Sch Biosci & Bioengn, Guangzhou 510006, Guangdong, Peoples R China
2.Peking Univ Hlth Sci Ctr, Inst Syst Biomed, Sch Basic Med Sci, Beijing 100191, Peoples R China
3.Peking Univ Hlth Sci Ctr, Dept Biophys, Sch Basic Med Sci, Beijing 100191, Peoples R China
4.S China Univ Technol, Coll Light Ind & Food Sci, Guangzhou 510641, Guangdong, Peoples R China

Recommended Citation:
Liu, Liang,Chen, Jiyun,Yang, Bo,et al. Crystal structure and function of an unusual dimeric Hsp20.1 provide insight into the thermal protection mechanism of small heat shock proteins[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2015,458(2):429-434.
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