Hsp90 and p23 Molecular Chaperones Control Chromatin Architecture by Maintaining the Functional Pool of the RSC Chromatin Remodeler

Frank J. Echtenkamp, Zlata Gvozdenov, Nicholas L. Adkins, Yang Zhang, Melinda Lynch-Day, Shinya Watanabe, Craig L. Peterson, Brian C. Freeman

Research output: Contribution to journalArticle


Molecular chaperones govern protein homeostasis, being allied to the beginning (folding) and ending (degradation) of the protein life cycle. Yet, the Hsp90 system primarily associates with native factors, including fully assembled complexes. The significance of these connections is poorly understood. To delineate why Hsp90 and its cochaperone p23 interact with a mature structure, we focused on the RSC chromatin remodeler. Both Hsp90 and p23 triggered the release of RSC from DNA or a nucleosome. Although Hsp90 only freed bound RSC, p23 enhanced nucleosome remodeling prior to discharging the complex. In vivo, RSC mobility and remodeling function were chaperone dependent. Our results suggest Hsp90 and p23 contribute to proteostasis by chaperoning mature factors through energetically unfavorable events, thereby maintaining the cellular pool of active native proteins. In the case of RSC, p23 and Hsp90 promote a dynamic action, allowing a limited number of remodelers to effectively maintain chromatin in a pliable state.

Original languageEnglish (US)
Pages (from-to)888-899
Number of pages12
JournalMolecular cell
Issue number5
StatePublished - Dec 1 2016



  • Hsp90
  • RSC
  • chromatin remodeling
  • molecular chaperones
  • p23
  • protein dynamics

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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