The C-terminal Helices of Heat Shock Protein 70 Are Essential for J-domain Binding and ATPase Activation
Gao, XC; Zhou, CJ; Zhou, ZR; Wu, M; Cao, CY; Hu, HY
刊名JOURNAL OF BIOLOGICAL CHEMISTRY
2012
卷号287期号:8页码:6044-6052
通讯作者Hu, HY (reprint author), Chinese Acad Sci, State Key Lab Mol Biol, Inst Biochem & Cell Biol, Shanghai Inst Biol Sci, Shanghai 200031, Peoples R China.,hyhu@sibs.ac.cn
英文摘要The J-domain co-chaperones work together with the heat shock protein 70 (HSP70) chaperone to regulate many cellular events, but the mechanism underlying the J-domain-mediated HSP70 function remains elusive. We studied the interaction between human-inducible HSP70 and Homo sapiens J-domain protein (HSJ1a), a J domain and UIM motif-containing co-chaperone. The J domain of HSJ1a shares a conserved structure with other J domains from both eukaryotic and prokaryotic species, and it mediates the interaction with and the ATPase cycle of HSP70. Our in vitro study corroborates that the N terminus of HSP70 including the ATPase domain and the substrate-binding beta-subdomain is not sufficient to bind with the J domain of HSJ1a. The C-terminal helical alpha-subdomain of HSP70, which was considered to function as a lid of the substrate-binding domain, is crucial for binding with the J domain of HSJ1a and stimulating the ATPase activity of HSP70. These fluctuating helices are likely to contribute to a proper conformation of HSP70 for J-domain binding other than directly bind with the J domain. Our findings provide an alternative mechanism of allosteric activation for functional regulation of HSP70 by its J-domain co-chaperones.
学科主题Biochemistry & Molecular Biology
类目[WOS]Biochemistry & Molecular Biology
关键词[WOS]MOLECULAR CHAPERONE DNAK ; SUBSTRATE-BINDING ; HSP70 CHAPERONES ; ALPHA-SYNUCLEIN ; NMR STRUCTURE ; RICH REGION ; PROTEIN ; HSP40 ; COCHAPERONE ; DYNAMICS
收录类别SCI
语种英语
WOS记录号WOS:000300638000077
内容类型期刊论文
版本出版稿
源URL[http://202.127.25.143/handle/331003/636]  
专题上海生化细胞研究所_上海生科院生化细胞研究所
推荐引用方式
GB/T 7714
Gao, XC,Zhou, CJ,Zhou, ZR,et al. The C-terminal Helices of Heat Shock Protein 70 Are Essential for J-domain Binding and ATPase Activation[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2012,287(8):6044-6052.
APA Gao, XC,Zhou, CJ,Zhou, ZR,Wu, M,Cao, CY,&Hu, HY.(2012).The C-terminal Helices of Heat Shock Protein 70 Are Essential for J-domain Binding and ATPase Activation.JOURNAL OF BIOLOGICAL CHEMISTRY,287(8),6044-6052.
MLA Gao, XC,et al."The C-terminal Helices of Heat Shock Protein 70 Are Essential for J-domain Binding and ATPase Activation".JOURNAL OF BIOLOGICAL CHEMISTRY 287.8(2012):6044-6052.
个性服务
查看访问统计
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。


©版权所有 ©2017 CSpace - Powered by CSpace