Hsp104 is a highly conserved protein with two essential nucleotide-binding sites

Nature. 1991 Sep 19;353(6341):270-3. doi: 10.1038/353270a0.

Abstract

Most eukaryotic cells produce proteins with relative molecular masses in the range of 100,000 to 110,000 after exposure to high temperatures. These proteins have been studied only in yeast and mammalian cells. In Saccharomyces cerevisiae, heat-shock protein hsp104 is vital for tolerance to heat, ethanol and other stresses. The mammalian hsp110 protein is nucleolar and redistributes with growth state, nutritional conditions and heat shock. The relationships between hsp110, hsp104 and the high molecular mass heat-shock proteins of other organisms were unknown. We report here that hsp104 is a member of the highly conserved ClpA/ClpB protein family first identified in Escherichia coli and that additional heat-inducible members of this family are present in Schizosaccharomyces pombe and in mammals. Mutagenesis of two putative nucleotide-binding sites in hsp104 indicates that both are essential for function in thermotolerance.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Escherichia coli / genetics
  • Fungal Proteins
  • Genes, Fungal*
  • HeLa Cells / physiology
  • Heat-Shock Proteins / genetics*
  • Humans
  • Molecular Sequence Data
  • RNA, Fungal / genetics
  • Rabbits
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / growth & development
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Nucleic Acid

Substances

  • Fungal Proteins
  • Heat-Shock Proteins
  • RNA, Fungal
  • Saccharomyces cerevisiae Proteins
  • HsP104 protein, S cerevisiae

Associated data

  • GENBANK/M67479