学科主题基础医学
Crystal structure and function of an unusual dimeric Hsp20.1 provide insight into the thermal protection mechanism of small heat shock proteins
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
2015-03-06
DOI10.1016/j.bbrc.2015.01.134
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
WOS记录号WOS:000351482200035
项目编号2014ZM0062 ; S2012040007734
资助机构Fundamental Research Funds for the Central Universities ; PhD Start-up Fund of Natural Science Foundation of Guangdong Province
引用统计
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/59934
专题北京大学基础医学院_北京大学系统生物医学研究所
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
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GB/T 7714
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.
APA Liu, Liang,Chen, Jiyun,Yang, Bo,&Wang, Yonghua.(2015).Crystal structure and function of an unusual dimeric Hsp20.1 provide insight into the thermal protection mechanism of small heat shock proteins.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,458(2),429-434.
MLA Liu, Liang,et al."Crystal structure and function of an unusual dimeric Hsp20.1 provide insight into the thermal protection mechanism of small heat shock proteins".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 458.2(2015):429-434.
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