Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth.

ABSTRACT: The Hsp90 chaperone is required for the maturation of signal transduction clients, including many kinases and nuclear steroid hormone receptors. The binding and hydrolysis of ATP by Hsp90 drive conformational rearrangements in three structure domains. Two intrinsically disordered regions of Hsp90 located between these domains and at the C terminus have traditionally been considered to impart flexibility. We discovered that the charged nature of these acid-rich disordered regions imparts a solubility-promoting function to Hsp90 that is important for its cellular activity in yeast. Both the solubility-promoting function and ATPase activity must occur in the same Hsp90 molecule in order to support robust growth, suggesting that the solubility-promoting function is required during the ATP-driv

SUBMITTER: Pursell NW 

PROVIDER: S-EPMC3416057 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature