Journal
NATURE COMMUNICATIONS
Volume 6, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms7655
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Funding
- CompInt program of the Elitenetzwerk Bayern
- Bavarian Ministry of Sciences, Research and the Arts (Bavarian Molecular Biosystems Research Network)
- Austrian Academy of Sciences (APART-fellowship)
- Deutsche Forschungsgemeinschaft (Emmy Noether program) [MA 5703/1-1]
- Studienstiftung des deutschen Volkes
- Research Foundation Flanders (FWO Vlaanderen)
- DFG via the Excellence initiative Center for Integrated Protein Science Munich (CIPSM)
- DFG via the Nano-systems Initative Munich (NIM)
- Ludwig-Maximilians-Universitat Munchen via the LMUInnovativ BioImaging Network
- Center for NanoScience
- [SFB 1035]
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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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