Affinity-purification and identification of GrpE homologues from mammalian mitochondria

Biochim Biophys Acta. 1995 Apr 5;1248(1):75-9. doi: 10.1016/0167-4838(95)00007-h.

Abstract

We used affinity chromatography on DnaK columns to identify a mitochondrial GrpE homologue from bovine, porcine and rat liver mitochondria. The 24 kDa GrpE homologue bound specifically to the DnaK column and was not eluted with 1 M KCl but readily with 5 mM ATP. Sequence analysis of the bovine homologue (85 residues) revealed 42% positional identity to mitochondrial GrpEp from S. cerevisiae and about 30% identity to the bacterial counterparts. Thus, GrpE homologues from higher and lower eukaryotes are highly conserved.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Fungal Proteins / chemistry
  • Fungal Proteins / isolation & purification*
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / isolation & purification*
  • Membrane Transport Proteins*
  • Mitochondria, Liver / metabolism*
  • Mitochondrial Membrane Transport Proteins
  • Molecular Chaperones
  • Molecular Sequence Data
  • Saccharomyces cerevisiae Proteins*
  • Sequence Homology, Amino Acid

Substances

  • Fungal Proteins
  • Heat-Shock Proteins
  • MGE1 protein, S cerevisiae
  • Membrane Transport Proteins
  • Mitochondrial Membrane Transport Proteins
  • Molecular Chaperones
  • Saccharomyces cerevisiae Proteins

Associated data

  • GENBANK/X58406