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DOI | 10.1038/s41467-019-12692-7 |
A switch point in the molecular chaperone Hsp90 responding to client interaction | |
Rutz, Daniel Andreas1; Luo, Qi1,2,3; Freiburger, Lee1,4; Madl, Tobias4,5; Kaila, Ville R. I.1; Sattler, Michael1,4; Buchner, Johannes1 | |
2019-10-11 | |
发表期刊 | NATURE COMMUNICATIONS |
ISSN | 2041-1723 |
出版年 | 2018 |
卷号 | 9 |
文章类型 | Article |
语种 | 英语 |
国家 | Germany; Peoples R China; Austria |
英文摘要 | Heat shock protein 90 (Hsp90) is a dimeric molecular chaperone that undergoes large conformational changes during its functional cycle. It has been established that conformational switch points exist in the N-terminal (Hsp90-N) and C-terminal (Hsp90-C) domains of Hsp90, however information for switch points in the large middle-domain (Hsp90-M) is scarce. Here we report on a tryptophan residue in Hsp90-M as a new type of switch point. Our study shows that this conserved tryptophan senses the interaction of Hsp90 with a stringent client protein and transfers this information via a cation-p interaction with a neighboring lysine. Mutations at this position hamper the communication between domains and the ability of a client protein to affect the Hsp90 cycle. The residue thus allows Hsp90 to transmit information on the binding of a client from Hsp90-M to Hsp90-N which is important for progression of the conformational cycle and the efficient processing of client proteins. |
领域 | 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000430056700004 |
WOS关键词 | ESCHERICHIA-COLI HSP90 ; CONFORMATIONAL DYNAMICS ; TYROSINE PHOSPHORYLATION ; SACCHAROMYCES-CEREVISIAE ; STRUCTURAL BIOLOGY ; TERMINAL DOMAIN ; ATP HYDROLYSIS ; PROTEIN ; BINDING ; MACHINERY |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/204588 |
专题 | 资源环境科学 |
作者单位 | 1.Tech Univ Munich, Dept Chem, Ctr Integrated Prot Sci, D-84748 Garching, Germany; 2.Zhejiang Univ, Soft Matter Res Ctr, Hangzhou 310027, Zhejiang, Peoples R China; 3.Zhejiang Univ, Dept Chem, Hangzhou 310027, Zhejiang, Peoples R China; 4.Helmholtz Zentrum Munchen, Inst Struct Biol, D-85764 Neuherberg, Germany; 5.Med Univ Graz, Mol Biol & Biochem, Gottfried Schatz Res Ctr Cell Signaling Metab & A, A-8010 Graz, Austria |
推荐引用方式 GB/T 7714 | Rutz, Daniel Andreas,Luo, Qi,Freiburger, Lee,et al. A switch point in the molecular chaperone Hsp90 responding to client interaction[J]. NATURE COMMUNICATIONS,2019,9. |
APA | Rutz, Daniel Andreas.,Luo, Qi.,Freiburger, Lee.,Madl, Tobias.,Kaila, Ville R. I..,...&Buchner, Johannes.(2019).A switch point in the molecular chaperone Hsp90 responding to client interaction.NATURE COMMUNICATIONS,9. |
MLA | Rutz, Daniel Andreas,et al."A switch point in the molecular chaperone Hsp90 responding to client interaction".NATURE COMMUNICATIONS 9(2019). |
条目包含的文件 | 条目无相关文件。 |
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