Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains

S. A. Teter, W. A. Houry, D. Ang, T. Tradler, D. Rockabrand, G. Fischer, P. Blum, C. Georgopoulos, F. U. Hartl

Research output: Contribution to journalArticle

317 Scopus citations

Abstract

A role for DnaK, the major E. coli Hsp70, in chaperoning de novo protein folding has remained elusive. Here we show that under nonstress conditions DnaK transiently associates with a wide variety of nascent and newly synthesized polypeptides, with a preference for chains larger than 30 kDa. Deletion of the nonessential gene encoding trigger factor, a ribosome- associated chaperone, results in a doubling of the fraction of nascent polypeptides interacting with DnaK. Combined deletion of the trigger factor and DnaK genes is lethal under normal growth conditions. These findings indicate important, partially overlapping functions of DnaK and trigger factor in de novo protein folding and explain why the loss of either chaperone can be tolerated by E. coli.

Original languageEnglish (US)
Pages (from-to)755-765
Number of pages11
JournalCell
Volume97
Issue number6
DOIs
StatePublished - Jan 1 1999

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Fingerprint Dive into the research topics of 'Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains'. Together they form a unique fingerprint.

  • Cite this

    Teter, S. A., Houry, W. A., Ang, D., Tradler, T., Rockabrand, D., Fischer, G., Blum, P., Georgopoulos, C., & Hartl, F. U. (1999). Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell, 97(6), 755-765. https://doi.org/10.1016/S0092-8674(00)80787-4