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

Author

Listed:
  • Alina Röhl

    (Technische Universität München)

  • Daniela Wengler

    (Center for Nano Science, Center for integrated protein science (CIPSM) and Nanosystems Initiative München (NIM), Ludwig-Maximilians-Universität München)

  • Tobias Madl

    (Technische Universität München
    Institute of Molecular Biology & Biochemistry, Center of Molecular Medicine, Medical University of Graz
    Institute of Structural Biology, Helmholtz Zentrum München)

  • Stephan Lagleder

    (Technische Universität München
    Institute for Advanced Study (IAS), Technische Universität München)

  • Franziska Tippel

    (Technische Universität München)

  • Monika Herrmann

    (Technische Universität München)

  • Jelle Hendrix

    (Center for Nano Science, Center for integrated protein science (CIPSM) and Nanosystems Initiative München (NIM), Ludwig-Maximilians-Universität München)

  • Klaus Richter

    (Technische Universität München)

  • Gordon Hack

    (Technische Universität München)

  • Andreas B. Schmid

    (Technische Universität München)

  • Horst Kessler

    (Technische Universität München
    Institute for Advanced Study (IAS), Technische Universität München
    Faculty of Science, King Abdulaziz University)

  • Don C. Lamb

    (Center for Nano Science, Center for integrated protein science (CIPSM) and Nanosystems Initiative München (NIM), Ludwig-Maximilians-Universität München)

  • Johannes Buchner

    (Technische Universität München)

Abstract

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.

Suggested Citation

  • Alina Röhl & Daniela Wengler & Tobias Madl & Stephan Lagleder & Franziska Tippel & Monika Herrmann & Jelle Hendrix & Klaus Richter & Gordon Hack & Andreas B. Schmid & Horst Kessler & Don C. Lamb & Joh, 2015. "Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules," Nature Communications, Nature, vol. 6(1), pages 1-14, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7655
    DOI: 10.1038/ncomms7655
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