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

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 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.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Rauch T,Hundley HA,Pfund C,Wegrzyn RD,Walter W,Kramer G,Kim SY,Craig EA,Deuerling E

doi

10.1111/j.1365-2958.2005.04690.x

subject

Has Abstract

pub_date

2005-07-01 00:00:00

pages

357-65

issue

2

eissn

0950-382X

issn

1365-2958

pii

MMI4690

journal_volume

57

pub_type

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