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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)
Verlagsversion DOI
Open Access Gold
Creative Commons Lizenzvertrag
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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Molecular Chaperone Hsp90; Wild-type P53; Tetratricopeptide Repeat; Saccharomyces-cerevisiae; Caenorhabditis-elegans; Photon Distribution; Co-chaperones; Protein; Hop; Complexes
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Zeitschrift Nature Communications
Quellenangaben Band: 6, Heft: , Seiten: , Artikelnummer: 6655 Supplement: ,
Verlag Nature Publishing Group
Verlagsort London
Begutachtungsstatus Peer reviewed