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A more recent version of this article appeared on August 1, 2002
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Submitted on April 3, 2002
Revised on May 22, 2002
Accepted on June 5, 2002
1 Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260
2 Department of Biochemistry, Mount Sinai School of Medicine, New York, NY 10029
* Corresponding author. E-mail address: jbrodsky{at}pitt.edu.
The S. cerevisiae Hsp40, Ydj1p, is involved in a variety of cellular activities that control polypeptide fate, such as folding and translocation across intracellular membranes. To elucidate the mechanism of Ydj1p action, and to identify functional partners, we screened for multicopy suppressors of the temperature-sensitive ydj1-151 mutant and identified a yeast Hsp110, SSE1. Over-expression of Sse1p also suppressed the folding defect of v-Src kinase in the ydj1-151 mutant, and partially reversed the 
-factor translocation defect. SSE1-dependent suppression of ydj1-151 thermosensitivity required a wild type ATP-binding domain of Sse1p. However, the Sse1p mutants maintained heat-denatured firefly luciferase in a folding-competent state in vitro and restored human androgen receptor folding in sse1 mutant cells. The folding of both v-Src kinase and human androgen receptor in yeast requires the Hsp90 complex. Together, these data suggest that Ydj1p and Sse1p are interacting co-chaperones in the Hsp90 complex and together facilitate Hsp-90 dependent activity.
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