Deep Structural Analysis of RPAP3 and PIH1D1, Two Components of the HSP90 Co-chaperone R2TP Complex

被引：37

作者：

Henri, Julien ^{[1
]}

Chagot, Marie-Eve ^{[2
]}

Bourguet, Maxime ^{[3
]}

Abel, Yoann ^{[4
]}

Terral, Guillaume ^{[3
]}

Maurizy, Chloe ^{[4
]}

Aigueperse, Christelle ^{[2
]}

Georgescauld, Florian ^{[1
]}

Vandermoere, Franck ^{[5
]}

Saint-Fort, Renette ^{[1
]}

Behm-Ansmant, Isabelle ^{[2
]}

Charpentier, Bruno ^{[2
]}

Pradet-Balade, Berengere ^{[6
]}

Verheggen, Celine ^{[4
]}

Bertrand, Edouard ^{[4
]}

Meyer, Philippe ^{[1
]}

Cianferani, Sarah ^{[3
]}

Manival, Xavier ^{[2
]}

Quinternet, Marc ^{[7
]}

机构：

[1] Sorbonne Univ, CNRS, IBPC, LBMCE,UMR 8226, F-75005 Paris, France

[2] Univ Lorraine, CNRS, IMoPA, F-54000 Nancy, France

[3] Univ Strasbourg, CNRS, IPHC, LSMBO,UMR 7178, F-67000 Strasbourg, France

[4] Univ Montpellier, CNRS, Equipe Labellise Ligue Contre Canc, IGMM,UMR 5535, F-34293 Montpellier, France

[5] Univ Montpellier, CNRS, INSERM, IGF, F-34094 Montpellier, France

[6] Univ Montpellier, CNRS, CRMB, UMR 5237, F-34000 Montpellier, France

[7] Univ Lorraine, CNRS, INSERM, IBSLor, F-54000 Nancy, France

来源：

STRUCTURE | 2018年 / 26卷 / 09期

关键词：

MOLECULAR CHAPERONE; PROTEIN; COCHAPERONE; PLATFORM; MODEL; PLUS;

D O I：

10.1016/j.str.2018.06.002

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：

RPAP3 and PIH1D1 are part of the HSP90 co-chaperone R2TP complex involved in the assembly process of many molecular machines. In this study, we performed a deep structural investigation of the HSP binding abilities of the two TPR domains of RPAP3. We combined 3D NMR, non-denaturing MS, and ITC techniques with Y2H, IP-LUMIER, FRET, and ATPase activity assays and explain the fundamental role played by the second TPR domain of RPAP3 in the specific recruitment of HSP90. We also established the 3D structure of an RPAP3: PIH1D1 sub-complex demonstrating the need for a 34-residue insertion, specific of RPAP3 isoform 1, for the tight binding of PIH1D1. We also confirm the existence of a complex lacking PIH1D1 in human cells (R2T), which shows differential binding to certain clients. These results highlight similarities and differences between the yeast and human R2TP complexes, and document the diversification of this family of co-chaperone complexes in human.

引用

页码：1196 / +

页数：22

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