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学科主题: 基础医学
题名:
Small heat shock protein AgsA forms dynamic fibrils
作者: Shi, Xiaodong2; Wang, Zhao1; Yan, Linxuan2; Ezemaduka, Anastasia N.2; Fan, Guizhen1; Wang, Rui3; Fu, Xinmiao2; Yin, Changcheng1; Chang, Zengyi2
关键词: Small heat shock protein ; Chaperone ; Fibril ; Amyloid ; Electron microscopy ; Cryo-electron tomography
刊名: FEBS LETTERS
发表日期: 2011-11-04
DOI: 10.1016/j.febslet.2011.09.042
卷: 585, 期:21, 页:3396-3402
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
研究领域[WOS]: Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
关键词[WOS]: CHAPERONE-LIKE ACTIVITY ; ESCHERICHIA-COLI ; BIOCHEMICAL-CHARACTERIZATION ; DENATURED PROTEIN ; CRYSTAL-STRUCTURE ; ALPHA-CRYSTALLIN ; AMYLOID FIBRILS ; IN-VITRO ; IBPB ; BINDING
英文摘要:

As a class of molecular chaperones, small heat shock proteins (sHsps) usually exist as multi-subunit spherical oligomers. In this study, we report that AgsA, a sHsp of Salmonella enterica serovar Typhimurium, spontaneously forms fibrils in vitro. These fibrils tend to be formed at elevated temperature and do not share the characteristics of amyloid. Interestingly, the fibril-forming AgsA is able to suppress the dithiothreitol-induced aggregation of insulin efficiently within a certain range of temperature. During this process, AgsA fibrils disappear and spherical complexes form between AgsA and insulin molecules. These data suggest that AgsA fibrils may represent a distinctive type of structural and functional form of sHsp from spherical oligomers. Our study provides new insights into sHsp structures and chaperone functions.

Structured summary of protein interactions:

AgsA and AgsA bind by electron microscopy (View interaction).

Insulin and Insulin bind by molecular sieving (View interaction).

Insulin and Insulin bind by electron microscopy (View interaction).

AgsA and AgsA bind by molecular sieving (View interaction).

AgsA and AgsA bind by fluorescence technology (View interaction).

AgsA and AgsA bind by circular dichroism (View interaction).

Insulin and Insulin bind by fluorescence technology (View interaction).

AgsA and Insulin bind by molecular sieving (View interaction).

AgsA and AgsA bind by electron tomography (View interaction). (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

语种: 英语
所属项目编号: 30570355 ; 30670022 ; 31170738 ; 31100559 ; 2006CB806508 ; 2006CB910300 ; 2006CB806501 ; 2010CB912404
项目资助者: National Natural Science Foundation of China ; National Key Basic Research Foundation of China
WOS记录号: WOS:000296575400008
Citation statistics:
内容类型: 期刊论文
版本: 出版稿
URI标识: http://ir.bjmu.edu.cn/handle/400002259/58321
Appears in Collections:基础医学院_生物物理学系_期刊论文

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作者单位: 1.Peking Univ, Hlth Sci Ctr, Dept Biophys, Beijing 100191, Peoples R China
2.Peking Univ, State Key Lab Prot & Plant Gene Res, Sch Life Sci, Beijing 100871, Peoples R China
3.Baylor Coll Med, Verna & Marrs McLean Dept Biochem & Mol Biol, Natl Ctr Macromol Imaging, Houston, TX 77030 USA

Recommended Citation:
Shi, Xiaodong,Wang, Zhao,Yan, Linxuan,et al. Small heat shock protein AgsA forms dynamic fibrils[J]. FEBS LETTERS,2011,585(21):3396-3402.
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