HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor

Mehdi Kabani, Catherine McLellan, Deborah A. Raynes, Vince Guerriero, Jeffrey L. Brodsky

Research output: Contribution to journalArticle

83 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)339-342
Number of pages4
JournalFEBS Letters
Volume531
Issue number2
DOIs
StatePublished - Nov 6 2002

Keywords

  • Fes1p
  • Hsc70
  • Hsp70
  • HspBP1
  • Nucleotide exchange
  • Sls1p

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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