A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides.
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.
Deshaies
R J
RJ
Department of Biochemistry, University of California, Berkeley 94720.
Koch
B D
BD
Werner-Washburne
M
M
Craig
E A
EA
Schekman
R
R
D005075:Biological Evolution; D001693:Biological Transport, Active; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000235:genetics / Q000502:physiology*; D000072235:Mating Factor; D008928:Mitochondria / Q000378:metabolism*; D008954:Models, Biological; D009693:Nucleic Acid Hybridization; D010455:Peptides / Q000235:genetics / Q000378:metabolism; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure
D006360:Heat-Shock Proteins; D010455:Peptides; D011498:Protein Precursors; D011506:Proteins; D000072235:Mating Factor