MOLECULARANDCELLULARBIOLOGY,创新.PDFVIP

MOLECULAR AND CELLULAR BIOLOGY, Nov. 2001, p. 7569–7575 Vol. 21, No. 22 0270-7306/01/$04.00 0 DOI: 10.1128/MCB.21.22.7569–7575.2001 Copyright © 2001, American Society for Microbiology. All Rights Reserved. Hsp104 Interacts with Hsp90 Cochaperones in Respiring Yeast ´ ´ TOUFIK ABBAS-TERKI, OLIVIER DONZE, PIERRE-ANDRE BRIAND, AND DIDIER PICARD* De´partement de Biologie Cellulaire, Universite´ de Gene`ve, Sciences III, CH-1211 Geneva 4, Switzerland Received 2 July 2001/Returned for modification 3 August 2001/Accepted 13 August 2001 The highly abundant molecular chaperone Hsp90 functions with assistance from auxiliary factors, collec- tively referred to as Hsp90 cochaperones, and the Hsp70 system. Hsp104, a molecular chaperone required for stress tolerance and for maintenance of [psi ] prions in the budding yeast Saccharomyces cerevisiae, appears to collaborate only with the Hsp70 system. We now report that several cochaperones previously thought to be dedicated to Hsp90 are shared with Hsp104. We show that the Hsp90 cochaperones Sti1, Cpr7, and Cns1, which utilize tetratricopeptide repeat (TPR) domains to interact with a common surface on Hsp90, form complexes with Hsp104 in vivo and that Sti1 and Cpr7 interact with Hsp104 directly in vitro. The interaction is Hsp90 independent, as further emphasized by the fact that two distinct TPR domains of Sti1 are required for binding D o