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J Biol Chem. 2014 Jun 20;289(25):17589-96. doi: 10.1074/jbc.M114.564989. Epub 2014 May 5.

Distinct roles for release factor 1 and release factor 2 in translational quality control.

Author information

1
From the Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 and.
2
the Department of Biology, Washington University in St. Louis, St. Louis, Missouri 63130 hzaher@wustl.edu.

Abstract

In bacteria, stop codons are recognized by two similar class 1 release factors, release factor 1 (RF1) and release factor 2 (RF2). Normally, during termination, the class 2 release factor 3 (RF3), a GTPase, functions downstream of peptide release where it accelerates the dissociation of RF1/RF2 prior to ribosome recycling. In addition to their canonical function in termination, both classes of release factor are also involved in a post peptidyl transfer quality control (post PT QC) mechanism where the termination factors recognize mismatched (i.e. error-containing) ribosome complexes and promote premature termination. Here, using a well defined in vitro system, we explored the role of release factors in canonical termination and post PT QC. As reported previously, during canonical termination, RF1 and RF2 recognize stop codons in a similar manner, and RF3 accelerates their rate of dissociation. During post PT QC, only RF2 (and not RF1) effectively binds to mismatched ribosome complexes; and whereas the addition of RF3 to RF2 increased its rate of release on mismatched complexes, the addition of RF3 to RF1 inhibited its rate of release but increased the rate of peptidyl-tRNA dissociation. Our data strongly suggest that RF2, in addition to its primary role in peptide release, functions as the principle factor for post PT QC.

KEYWORDS:

Protein Synthesis; Ribosome; Translation; Translation Control; Translation Release Factor

PMID:
24798339
PMCID:
PMC4067194
DOI:
10.1074/jbc.M114.564989
[Indexed for MEDLINE]
Free PMC Article

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