National Changhua University of Education Institutional Repository : Item 987654321/11477
English  |  正體中文  |  简体中文  |  全文筆數/總筆數 : 6507/11669
造訪人次 : 30132186      線上人數 : 454
RC Version 3.2 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜尋範圍 進階搜尋

請使用永久網址來引用或連結此文件: http://ir.ncue.edu.tw/ir/handle/987654321/11477

題名: Conformations of the Nucleotide and Polypeptide Binding Domains of a Cytosolic Hsp70 Molecular Chaperone Are Coupled
作者: Fung, Katie L.;Hilgenberg, Lutz;Wang, Nancy M.;Chirico, William J.
貢獻者: 生物技術研究所
日期: 1996-08
上傳時間: 2012-06-06T02:02:52Z
出版者: American Society for Biochemistry and Molecular Biology
摘要: 70-kDa heat shock protein (Hsp70) molecular chaperones are ATPases that participate in protein folding by regulating protein-protein interactions. ATP binds to the highly conserved amino-terminal domain, whereas polypeptides bind to the less conserved carboxyl-terminal domain. These domains are functionally coupled. Polypeptides were previously shown to dissociate from Hsp70s upon ATP binding and to stimulate ATPase activity. We probed the structure of the yeast cytosolic Hsp70 Ssa1p using limited proteolysis to determine whether the conformations of its nucleotide and polypeptide binding domains are also coupled. Ssa1p adopted three distinct conformations, nucleotide-free, ADP-dependent, and ATP-dependent. Complete conformational changes required K+ and Mg2+. Using amino-terminal sequencing, ATP-agarose chromatography, and a carboxyl-terminal-specific antibody, we mapped the locations of the major proteolytic fragments. Nucleotides altered the conformations of both the nucleotide and polypeptide binding domains. Similarly, a polypeptide altered the conformations of both domains. These results indicate that the conformations of the nucleotide and polypeptide binding domains are coupled.
關聯: Journal of Biological Chemistry, 271(35): 21559-21565
顯示於類別:[生物技術研究所] 期刊論文

文件中的檔案:

檔案 大小格式瀏覽次數
index.html0KbHTML615檢視/開啟


在NCUEIR中所有的資料項目都受到原著作權保護.

 

DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - 回饋