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Advanced filters: Author: Alina Röhl Clear advanced filters

  • The chaperones Hsp70 and Hsp90 are physically linked via the cochaperone Sti1/Hop, that has two binding sites for Hsp70. Here, Röhl et al.show that binding of Hsp90 changes the conformation of Sti1/Hop and determines to which site Hsp70 binds, perhaps facilitating transfer of client proteins from Hsp70 to Hsp90.

    • Alina Röhl
    • Daniela Wengler
    • Johannes Buchner
    ResearchOpen Access
    Nature Communications
    Volume: 6, P: 1-14

  • Hsp70 and Hsp90 cooperate to fold client proteins, aided by co-chaperones such as Hop. Here Alvira et al. determine EM structures of various combinations of Hsp70, Hsp90, Hop and a client protein to shed structural insight into the mechanism of client protein transfer from one chaperone to the other.

    • Sara Alvira
    • Jorge Cuéllar
    • José M. Valpuesta
    Research
    Nature Communications
    Volume: 5, P: 1-13