Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways.
The substrate-specific protein chaperone Hsp90 (heat shock protein 90) from Saccharomyces cerevisiae functions in diverse signal transduction pathways. A mutation in YDJ1, a member of the DnaJ chaperone family, was recovered in a synthetic-lethal screen with Hsp90 mutants. In an otherwise wild-type background, the ydj1 mutation exerted strong and specific ... effects on three Hsp90 substrates, derepressing two (the estrogen and glucocorticoid receptors) and reducing the function of the third (the tyrosine kinase p60v-src). Analysis of one of these substrates, the glucocorticoid receptor, indicated that Ydj1 exerts its effects through physical interaction with Hsp90 substrates.
Mesh Terms:
Base Sequence, Fungal Proteins, HSP40 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Heat-Shock Proteins, Molecular Chaperones, Molecular Sequence Data, Oncogene Protein pp60(v-src), Point Mutation, Protein Conformation, Receptors, Estrogen, Receptors, Glucocorticoid, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Signal Transduction
Base Sequence, Fungal Proteins, HSP40 Heat-Shock Proteins, HSP90 Heat-Shock Proteins, Heat-Shock Proteins, Molecular Chaperones, Molecular Sequence Data, Oncogene Protein pp60(v-src), Point Mutation, Protein Conformation, Receptors, Estrogen, Receptors, Glucocorticoid, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Signal Transduction
Science
Date: Jun. 02, 1995
PubMed ID: 7761857
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