« Previous AbstractValproate inhibits MAP kinase signalling and cell cycle progression in S. cerevisiae    Next AbstractSwitch-domain mutations in the Saccharomyces cerevisiae G protein alpha-subunit Gpa1p identify a receptor subtype-biased mating defect »

Nature

Title:		A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
Author(s):		Deshaies RJ; Koch BD; Werner-Washburne M; Craig EA; Schekman R;
Address:		"Department of Biochemistry, University of California, Berkeley 94720"
Journal Title:		Nature
Year:		1988
Volume:		332
Issue:		6167
Page Number:		800 - 805
DOI:		10.1038/332800a0
ISSN/ISBN:		0028-0836 (Print) 0028-0836 (Linking)
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
Keywords:		"Biological Evolution Biological Transport, Active Endoplasmic Reticulum/metabolism Heat-Shock Proteins/genetics/*physiology Mating Factor Mitochondria/*metabolism Models, Biological Nucleic Acid Hybridization Peptides/genetics/metabolism Protein Precursor;"
Notes:		"MedlineDeshaies, R J Koch, B D Werner-Washburne, M Craig, E A Schekman, R eng GM26755/GM/NIGMS NIH HHS/ GM36881/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. England 1988/04/28 Nature. 1988 Apr 28; 332(6167):800-5. doi: 10.1038/332800a0"