A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

Nature. 1988 Apr 28;332(6167):800-5. doi: 10.1038/332800a0.

Abstract

Depletion of a subset of 70K stress proteins in yeast mutants shows that they are involved in the post-translational import of precursor polypeptides into both mitochondria and the lumen of the endoplasmic reticulum. The identification of such a basic function may explain the remarkable evolutionary conservation of the gene family encoding these proteins.

Publication types

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

MeSH terms

  • Biological Evolution
  • Biological Transport, Active
  • Endoplasmic Reticulum / metabolism
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / physiology*
  • Mating Factor
  • Mitochondria / metabolism*
  • Models, Biological
  • Nucleic Acid Hybridization
  • Peptides / genetics
  • Peptides / metabolism
  • Protein Precursors / metabolism*
  • Protein Processing, Post-Translational
  • Proteins / metabolism*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae / ultrastructure

Substances

  • Heat-Shock Proteins
  • Peptides
  • Protein Precursors
  • Proteins
  • Mating Factor