Premium
Dissecting functional similarities of ribosome‐associated chaperones from Saccharomyces cerevisiae and Escherichia coli
Author(s) -
Rauch Thomas,
Hundley Heather A.,
Pfund Chris,
Wegrzyn Renee D.,
Walter William,
Kramer Günter,
Kim SoYoung,
Craig Elizabeth A.,
Deuerling Elke
Publication year - 2005
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2005.04690.x
Subject(s) - biology , ribosome , escherichia coli , saccharomyces cerevisiae , yeast , ribosomal protein , ribosomal rna , eukaryotic ribosome , biochemistry , genetics , microbiology and biotechnology , rna , gene
Summary 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 Rpl25 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.