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Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop

Author

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  • Sara Alvira

    (Centro Nacional de Biotecnología (CNB-CSIC), Darwin, 3
    Present address: School of Biochemistry, University of Bristol, Bristol BS8 1TD , UK)

  • Jorge Cuéllar

    (Centro Nacional de Biotecnología (CNB-CSIC), Darwin, 3)

  • Alina Röhl

    (Technische Universität München)

  • Soh Yamamoto

    (Faculty and Graduate School of Engineering and Resource Science, Akita University
    Sapporo Medical University School of Medicine)

  • Hideaki Itoh

    (Faculty and Graduate School of Engineering and Resource Science, Akita University)

  • Carlos Alfonso

    (Centro de Investigaciones Biológicas (CIB-CSIC), Ramiro de Maetzu 9)

  • Germán Rivas

    (Centro de Investigaciones Biológicas (CIB-CSIC), Ramiro de Maetzu 9)

  • Johannes Buchner

    (Technische Universität München)

  • José M. Valpuesta

    (Centro Nacional de Biotecnología (CNB-CSIC), Darwin, 3)

Abstract

In eukarya, chaperones Hsp70 and Hsp90 act coordinately in the folding and maturation of a range of key proteins with the help of several co-chaperones, especially Hop. Although biochemical data define the Hop-mediated Hsp70–Hsp90 substrate transfer mechanism, the intrinsic flexibility of these proteins and the dynamic nature of their complexes have limited the structural studies of this mechanism. Here we generate several complexes in the Hsp70/Hsp90 folding pathway (Hsp90:Hop, Hsp90:Hop:Hsp70 and Hsp90:Hop:Hsp70 with a fragment of the client protein glucocorticoid receptor (GR-LBD)), and determine their 3D structure using electron microscopy techniques. Our results show that one Hop molecule binds to one side of the Hsp90 dimer in both extended and compact conformations, through Hop domain rearrangement that take place when Hsp70 or Hsp70:GR-LBD bind to Hsp90:Hop. The compact conformation of the Hsp90:Hop:Hsp70:GR-LBD complex shows that GR-LBD binds to the side of the Hsp90 dimer opposite the Hop attachment site.

Suggested Citation

  • Sara Alvira & Jorge Cuéllar & Alina Röhl & Soh Yamamoto & Hideaki Itoh & Carlos Alfonso & Germán Rivas & Johannes Buchner & José M. Valpuesta, 2014. "Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop," Nature Communications, Nature, vol. 5(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6484
    DOI: 10.1038/ncomms6484
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    Cited by:

    1. Antonia Moll & Lisa Marie Ramirez & Momchil Ninov & Juliane Schwarz & Henning Urlaub & Markus Zweckstetter, 2022. "Hsp multichaperone complex buffers pathologically modified Tau," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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