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Röhl, A.* ; Wengler, D.* ; Madl, T. ; Lagleder, S.* ; Tippel, F.* ; Hermann, M.* ; Hendrix, J.* ; Richter, K.* ; Hack, G.* ; Schmid, A.B.* ; Kessler, H.* ; Lamb, D.C.* ; Buchner, J.*

Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.

Nat. Commun. 6:6655 (2015)
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The cochaperone Sti1/Hop physically links Hsp70 and Hsp90. The protein exhibits one binding site for Hsp90 (TPR2A) and two binding sites for Hsp70 (TPR1 and TPR2B). How these sites are used remained enigmatic. Here we show that Sti1 is a dynamic, elongated protein that consists of a flexible N-terminal module, a long linker and a rigid C-terminal module. Binding of Hsp90 and Hsp70 regulates the Sti1 conformation with Hsp90 binding determining with which site Hsp70 interacts. Without Hsp90, Sti1 is more compact and TPR2B is the high-affinity interaction site for Hsp70. In the presence of Hsp90, Hsp70 shifts its preference. The linker connecting the two modules is crucial for the interaction with Hsp70 and for client activation in vivo. Our results suggest that the interaction of Hsp70 with Sti1 is tightly regulated by Hsp90 to assure transfer of Hsp70 between the modules, as a prerequisite for the efficient client handover.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Molecular Chaperone Hsp90; Wild-type P53; Tetratricopeptide Repeat; Saccharomyces-cerevisiae; Caenorhabditis-elegans; Photon Distribution; Co-chaperones; Protein; Hop; Complexes
Language english
Publication Year 2015
HGF-reported in Year 2015
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Journal Nature Communications
Quellenangaben Volume: 6, Issue: , Pages: , Article Number: 6655 Supplement: ,
Publisher Nature Publishing Group
Publishing Place London
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)
POF-Topic(s) 30505 - New Technologies for Biomedical Discoveries
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-552800-001
PubMed ID 25851214
DOI 10.1038/ncomms7655
WOS ID WOS:000353697200001
Scopus ID 84926615158
Erfassungsdatum 2015-04-10
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