Inhibitory effects of HSP70 chaperones on nascent polypeptides
نویسندگان
چکیده
منابع مشابه
Protein biogenesis: Chaperones for nascent polypeptides
A number of molecular chaperones have been found to interact with nascent polypeptides attached to ribosomes, allowing these protein-synthesis machines to play a key part in protein folding and targeting.
متن کاملComplexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells.
Folding of newly synthesized proteins in vivo is believed to be facilitated by the cooperative interaction of a defined group of proteins known as molecular chaperones. We investigated the direct interaction of chaperones with nascent polypeptides in the cytosol of mammalian cells by multiple methods. A new approach using a polyclonal antibody to puromycin allowed us to tag and capture a popula...
متن کاملHeat shock gene regulation by nascent polypeptides and denatured proteins: hsp70 as a potential autoregulatory factor
Heat shock genes encode proteins (hsp's) that play important structural roles under normal circumstances and are essential to the cells' ability to survive environmental insults. Evidence is presented herein that transcriptional regulation of hsp gene expression is linked with the regulation of overall protein synthesis as well as with the accumulation of proteins denatured by stressful events....
متن کاملPathways of allosteric regulation in Hsp70 chaperones
Central to the protein folding activity of Hsp70 chaperones is their ability to interact with protein substrates in an ATP-controlled manner, which relies on allosteric regulation between their nucleotide-binding (NBD) and substrate-binding domains (SBD). Here we dissect this mechanism by analysing mutant variants of the Escherichia coli Hsp70 DnaK blocked at distinct steps of allosteric commun...
متن کاملFunctional specificity among Hsp70 molecular chaperones.
Molecular chaperones of the 70-kilodalton heat shock protein (Hsp70) class bind to partially unfolded polypeptide substrates and participate in a wide variety of cellular processes. Differences in peptide-binding specificity among Hsp70s have led to the hypothesis that peptide binding determines specific Hsp70 functions. Protein domains were identified that were required for two separate functi...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1992
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.5560010803