A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
- 1 April 1988
- journal article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 332 (6167), 800-805
- https://doi.org/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.Keywords
This publication has 59 references indexed in Scilit:
- Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae.Molecular and Cellular Biology, 1987
- SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth.Proceedings of the National Academy of Sciences of the United States of America, 1987
- THE HEAT-SHOCK RESPONSEAnnual Review of Biochemistry, 1986
- Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas.The Journal of cell biology, 1986
- Uncoating ATPase is a member of the 70 kilodalton family of stress proteinsCell, 1986
- Rapid purification of mammalian 70,000-dalton stress proteins: affinity of the proteins for nucleotides.Molecular and Cellular Biology, 1985
- The Heat Shock ResponsCritical Reviews in Biochemistry, 1985
- An enzyme that removes clathrin coats: purification of an uncoating ATPase.The Journal of cell biology, 1984
- Major heat shock gene of Drosophila and the Escherichia coli heat-inducible dnaK gene are homologous.Proceedings of the National Academy of Sciences of the United States of America, 1984
- Saccharomyces cerevisiae contains a complex multigene family related to the major heat shock-inducible gene of Drosophila.Molecular and Cellular Biology, 1982