Fraction of nascent polypeptides associated with Hsp70 SSB

Range ~45 %
Organism Budding yeast Saccharomyces cerevisiae
Reference Wang F, Durfee LA, Huibregtse JM. A cotranslational ubiquitination pathway for quality control of misfolded proteins. Mol Cell. 2013 May 9 50(3):368-78. doi: 10.1016/j.molcel.2013.03.009. p.376 left column 2nd paragraphPubMed ID23583076
Primary Source F. Willmund et al., The cotranslational function of ribosome-associated Hsp70 in eukaryotic protein homeostasis, Cell, 152 (2013), pp. 196–209 doi: 10.1016/j.cell.2012.12.001.PubMed ID23332755
Method Primary source abstract: "Here, [investigators] use a sensitive and global approach to define the cotranslational substrate specificity of the yeast Hsp70 SSB."
Comments P.376 left column 2nd paragraph: "In yeast, Hsp70 SSB associates with approximately 45% of nascent polypeptides (primary source), consistent with the possibility that the relationship between nascent chain misfolding and ubiquitination may affect an incredibly broad range of cellular proteins."
Entered by Uri M
ID 113361