High-Resolution Structural Analysis Shows How Tah1 Tethers Hsp90 to the R2TP Complex

被引：38

作者：

Back, Regis ^{[1
]}

Dominguez, Cyril ^{[2
]}

Rothe, Benjamin ^{[1
]}

Bobo, Claude ^{[1
]}

Beaufils, Chrystel ^{[3
]}

Morera, Solange ^{[4
]}

Meyer, Philippe ^{[4
]}

Charpentier, Bruno ^{[1
]}

Branlant, Christiane ^{[1
]}

Allain, Frederic H. -T. ^{[2
]}

Manival, Xavier ^{[1
]}

机构：

[1] Univ Lorraine, CNRS, Biopole Univ Lorraine, Ingn Mol & Physiopathol Articulaire IMoPA,UMR 736, F-54505 Vandoeuvre Les Nancy, France

[2] ETH, Inst Mol Biol & Biophys IMB, CH-8093 Zurich, Switzerland

[3] UMR CNRS INPL 7568, LCPM, Grp Synth Organ & Biostruct, F-54001 Nancy, France

[4] UPR CNRS 3082, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France

来源：

STRUCTURE | 2013年 / 21卷 / 10期

关键词：

TETRATRICOPEPTIDE REPEAT DOMAIN; NMR STRUCTURE DETERMINATION; SACCHAROMYCES-CEREVISIAE; LIGAND-DISCRIMINATION; PROTEIN; CHAPERONE; COCHAPERONE; BINDING; IDENTIFICATION; MECHANISM;

D O I：

10.1016/j.str.2013.07.024

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The ubiquitous Hsp90 chaperone participates in snoRNP and RNA polymerase assembly through interaction with the R2TP complex. This complex includes the proteins Tah1, Pih1, Rvb1, and Rvb2. Tah1 bridges Hsp90 to R2TP. Its minimal TPR domain includes two TPR motifs and a capping helix. We established the high-resolution solution structures of Tah1 free and in complex with the Hsp90 C-terminal peptide. The TPR fold is similar in the free and bound forms and we show experimentally that in addition to its solvating/stabilizing role, the capping helix is essential for the recognition of the Hsp90 (EMEEVD709)-E-704 motif. In addition to Lys79 and Arg83 from the carboxylate clamp, this helix bears Tyr82 forming a pi/S-CH3 interaction with Hsp90 M-705 from the peptide 310 helix. The Tah1 C-terminal region is unfolded, and we demonstrate that it is essential for the recruitment of the Pih1 C-terminal domain and folds upon binding.

引用

页码：1834 / 1847

页数：14

共 40 条

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