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Molecular and Cellular Biology, July 2002, p. 4677-4689, Vol. 22, No. 13
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.13.4677-4689.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Nucleotide Exchange Factor for the Yeast Hsp70 Molecular Chaperone Ssa1p

Mehdi Kabani,1 Jean-Marie Beckerich,2 and Jeffrey L. Brodsky1*

Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260,1 Laboratoire de Génétique Moléculaire et Cellulaire, INRA, INA.PG, CNRS, 78850 Thiverval-Grignon, France2

Received 9 November 2001/ Returned for modification 9 January 2002/ Accepted 10 April 2002

We report on the identification of Fes1p (yBR101cp) as a cytosolic homologue of Sls1p, an endoplasmic reticulum (ER) protein previously shown to act as a nucleotide exchange factor for yeast BiP (M. Kabani, J.-M. Beckerich, and C. Gaillardin, Mol. Cell. Biol. 20:6923-6934, 2000). We found that Fes1p associates preferentially to the ADP-bound form of the cytosolic Hsp70 molecular chaperone Ssa1p and promotes nucleotide release. Fes1p activity was shown to be compartment and species specific since Sls1p and Escherichia coli GrpE could not substitute for Fes1p. Surprisingly, whereas Sls1p stimulated the ATPase activity of BiP in cooperation with luminal J proteins, Fes1p was shown to inhibit the Ydj1p-mediated activation of Ssa1p ATPase activity in steady-state and single-turnover assays. Disruption of FES1 in several wild-type backgrounds conferred a strong thermosensitive phenotype but partially rescued ydj1-151 thermosensitivity. The {Delta}fes1 strain was proficient for posttranslational protein translocation, as well as for the ER-associated degradation of two substrates. However, the {Delta}fes1 mutant showed increased cycloheximide sensitivity and a general translational defect, suggesting that Fes1p acts during protein translation, a process in which Ssa1p and Ydj1p are known to be involved. In support of this hypothesis, Fes1p was found to be associated with ribosomes.

* Corresponding author. Mailing address: Department of Biological Sciences, 267 Crawford Hall, University of Pittsburgh, Pittsburgh, PA 15260. Phone: (412) 624-4831. Fax: (412) 624-4759. E-mail: jbrodsky{at}pitt.edu.

Molecular and Cellular Biology, July 2002, p. 4677-4689, Vol. 22, No. 13
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.13.4677-4689.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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