Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli

Thomas Rauch, Heather A. Hundley, Chris Pfund, Renee D. Wegrzyn, William Walter, Günter Kramer, So Young Kim, Elizabeth A. Craig, Elke Deuerling

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

Ribosome-tethered chaperones that interact with nascent polypeptide chains have been identified in both prokaryotic and eukaryotic systems. However, these ribosome-associated chaperones share no sequence similarity: bacterial trigger factors (TF) form an independent protein family while the yeast machinery is Hsp70-based. The absence of any component of the yeast machinery results in slow growth at low temperatures and sensitivity to aminoglycoside protein synthesis inhibitors. After establishing that yeast ribosomal protein Rp125 is able to recruit TF to ribosomes when expressed in place of its Escherichia coli homologue L23, the ribosomal TF tether, we tested whether such divergent ribosome-associated chaperones are functionally interchangeable. E. coli TF was expressed in yeast cells that lacked the endogenous ribosome-bound machinery. TF associated with yeast ribosomes, cross-linked to yeast nascent polypeptides and partially complemented the aminoglycoside sensitivity, demonstrating that ribosome-associated chaperones from divergent organisms share common functions, despite their lack of sequence similarity.

Original languageEnglish (US)
Pages (from-to)357-365
Number of pages9
JournalMolecular Microbiology
Volume57
Issue number2
DOIs
StatePublished - Jul 1 2005

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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    Rauch, T., Hundley, H. A., Pfund, C., Wegrzyn, R. D., Walter, W., Kramer, G., Kim, S. Y., Craig, E. A., & Deuerling, E. (2005). Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli. Molecular Microbiology, 57(2), 357-365. https://doi.org/10.1111/j.1365-2958.2005.04690.x