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HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor
Author(s) -
Kabani Mehdi,
McLellan Catherine,
Raynes Deborah A,
Guerriero Vince,
Brodsky Jeffrey L
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03570-6
Subject(s) - nucleotide , endoplasmic reticulum , chaperone (clinical) , cytoplasm , yeast , biology , biochemistry , gene , guanine nucleotide exchange factor , homologous chromosome , saccharomyces cerevisiae , microbiology and biotechnology , chemistry , signal transduction , medicine , pathology
The yeast FES1 and SLS1 genes encode conserved nucleotide exchange factors that act on the cytoplasmic and endoplasmic reticulum luminal Hsp70s, Ssa1p and BiP, respectively. We report here that mammalian HspBP1 is homologous to Fes1p and that HspBP1 promotes nucleotide dissociation from both Ssa1p and mammalian Hsc70. In contrast, Fes1p inefficiently strips nucleotide from mammalian Hsc70, and unlike HspBP1 does not inhibit chaperone‐mediated protein refolding in vitro. Together, our data indicate that HspBP1 is a member of this new class of nucleotide exchange factors that exhibit varying degrees of compartment and species specificity.