PMID- 24798339 OWN - NLM STAT- MEDLINE DCOM- 20141006 LR - 20211021 IS - 1083-351X (Electronic) IS - 0021-9258 (Print) IS - 0021-9258 (Linking) VI - 289 IP - 25 DP - 2014 Jun 20 TI - Distinct roles for release factor 1 and release factor 2 in translational quality control. PG - 17589-96 LID - 10.1074/jbc.M114.564989 [doi] AB - 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. CI - (c) 2014 by The American Society for Biochemistry and Molecular Biology, Inc. FAU - Petropoulos, Alexandros D AU - Petropoulos AD AD - From the Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 and. FAU - McDonald, Megan E AU - McDonald ME AD - From the Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 and. FAU - Green, Rachel AU - Green R AD - From the Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 and. FAU - Zaher, Hani S AU - Zaher HS AD - the Department of Biology, Washington University in St. Louis, St. Louis, Missouri 63130 hzaher@wustl.edu. LA - eng GR - R00 GM094210/GM/NIGMS NIH HHS/United States GR - HHMI/Howard Hughes Medical Institute/United States GR - R01 GM059425/GM/NIGMS NIH HHS/United States GR - R00GM094210/GM/NIGMS NIH HHS/United States GR - R01GM059425-06A1/GM/NIGMS NIH HHS/United States PT - Journal Article PT - Research Support, N.I.H., Extramural PT - Research Support, Non-U.S. Gov't DEP - 20140505 PL - United States TA - J Biol Chem JT - The Journal of biological chemistry JID - 2985121R RN - 0 (Escherichia coli Proteins) RN - 0 (Peptide Termination Factors) RN - 0 (prfA protein, E coli) RN - 0 (prfB protein, E coli) SB - IM MH - Escherichia coli/genetics/*metabolism MH - Escherichia coli Proteins/genetics/*metabolism MH - Peptide Chain Termination, Translational/*physiology MH - Peptide Termination Factors/genetics/*metabolism MH - Ribosomes/genetics/*metabolism PMC - PMC4067194 OTO - NOTNLM OT - Protein Synthesis OT - Ribosome OT - Translation OT - Translation Control OT - Translation Release Factor EDAT- 2014/05/07 06:00 MHDA- 2014/10/07 06:00 PMCR- 2015/06/20 CRDT- 2014/05/07 06:00 PHST- 2014/05/07 06:00 [entrez] PHST- 2014/05/07 06:00 [pubmed] PHST- 2014/10/07 06:00 [medline] PHST- 2015/06/20 00:00 [pmc-release] AID - S0021-9258(20)40600-3 [pii] AID - M114.564989 [pii] AID - 10.1074/jbc.M114.564989 [doi] PST - ppublish SO - J Biol Chem. 2014 Jun 20;289(25):17589-96. doi: 10.1074/jbc.M114.564989. Epub 2014 May 5.