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学科主题基础医学
Small heat shock protein AgsA forms dynamic fibrils
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
2011-11-04
DOI10.1016/j.febslet.2011.09.042
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
WOS记录号WOS:000296575400008
引用统计
被引频次:8[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
版本出版稿
条目标识符http://ir.bjmu.edu.cn/handle/400002259/58321
专题北京大学基础医学院_生物物理学系
北京大学基础医学院
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
推荐引用方式
GB/T 7714
Shi, Xiaodong,Wang, Zhao,Yan, Linxuan,et al. Small heat shock protein AgsA forms dynamic fibrils[J]. FEBS LETTERS,2011,585(21):3396-3402.
APA Shi, Xiaodong.,Wang, Zhao.,Yan, Linxuan.,Ezemaduka, Anastasia N..,Fan, Guizhen.,...&Chang, Zengyi.(2011).Small heat shock protein AgsA forms dynamic fibrils.FEBS LETTERS,585(21),3396-3402.
MLA Shi, Xiaodong,et al."Small heat shock protein AgsA forms dynamic fibrils".FEBS LETTERS 585.21(2011):3396-3402.
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