PMID- 25636454
OWN - NLM
STAT- MEDLINE
DCOM- 20151026
LR  - 20181113
IS  - 1617-4623 (Electronic)
IS  - 1617-4623 (Linking)
VI  - 290
IP  - 4
DP  - 2015 Aug
TI  - Interactions of release factor RF3 with the translation machinery.
PG  - 1335-44
LID - 10.1007/s00438-015-0994-x [doi]
AB  - The bacterial release factor RF3 is a GTPase that has been implicated in 
      multiple, incompletely understood steps of protein synthesis. This study explores 
      the genetic interaction of RF3 with other components of the translation 
      machinery. RF3 contributes to translation termination by recycling the class I 
      release factors RF1 and RF2 off post-termination ribosomes. RF3 has also been 
      implicated in dissociation of peptidyl-tRNAs from elongating ribosomes and in a 
      post-peptidyltransferase quality control (post-PT QC) mechanism that selectively 
      terminates ribosomes carrying erroneous peptides. A majority of the in vivo 
      studies on RF3 have been carried out in K-12 strains of Escherichia coli which 
      carry a partially defective RF2 protein with an Ala to Thr substitution at 
      position 246. Here, the contribution of the K-12 specific RF2 variant to RF3 
      activities has been investigated. Strain reconstruction experiments in both E. 
      coli and Salmonella enterica demonstrate that defects in termination and post-PT 
      QC that are associated with RF3 loss, as well as phenotypes uncovered by 
      phenotypic profiling, are all substantially ameliorated when the incompletely 
      active K-12-specific RF2 protein is replaced by a fully active Ala246 RF2. These 
      results indicate that RF3 loss is well tolerated in bacteria with fully active 
      class I release factors, but that many of the previously reported phenotypes for 
      RF3 deletion strains have been compromised by the presence of a partially 
      defective RF2.
FAU - O'Connor, Michael
AU  - O'Connor M
AD  - School of Biological Sciences, University of Missouri-Kansas City, 5007 Rockhill 
      Rd., Kansas City, MO, 64110, USA, oconnormi@umkc.edu.
LA  - eng
PT  - Journal Article
DEP - 20150131
PL  - Germany
TA  - Mol Genet Genomics
JT  - Molecular genetics and genomics : MGG
JID - 101093320
RN  - 0 (Anti-Bacterial Agents)
RN  - 0 (Bacterial Proteins)
RN  - 0 (Escherichia coli Proteins)
RN  - 0 (Peptide Termination Factors)
RN  - 0 (RNA, Transfer, Amino Acyl)
RN  - 0 (prfA protein, E coli)
RN  - 0 (prfB protein, E coli)
RN  - 0 (prfC protein, E coli)
RN  - 0 (tRNA, peptidyl-)
RN  - OV42LHE42B (Cefsulodin)
SB  - IM
MH  - Anti-Bacterial Agents/pharmacology
MH  - Bacterial Proteins/genetics/metabolism
MH  - Cefsulodin/pharmacology
MH  - Escherichia coli/genetics/growth & development/*metabolism
MH  - Escherichia coli Proteins/genetics/*metabolism
MH  - Microbial Viability/drug effects/genetics
MH  - Mutation
MH  - Peptide Chain Termination, Translational
MH  - Peptide Termination Factors/genetics/*metabolism
MH  - Phenotype
MH  - Protein Binding
MH  - *Protein Biosynthesis
MH  - RNA, Transfer, Amino Acyl/genetics/metabolism
MH  - Ribosomes/metabolism
MH  - Salmonella enterica/genetics/growth & development/metabolism
EDAT- 2015/02/01 06:00
MHDA- 2015/10/27 06:00
CRDT- 2015/02/01 06:00
PHST- 2014/10/14 00:00 [received]
PHST- 2015/01/09 00:00 [accepted]
PHST- 2015/02/01 06:00 [entrez]
PHST- 2015/02/01 06:00 [pubmed]
PHST- 2015/10/27 06:00 [medline]
AID - 10.1007/s00438-015-0994-x [doi]
PST - ppublish
SO  - Mol Genet Genomics. 2015 Aug;290(4):1335-44. doi: 10.1007/s00438-015-0994-x. Epub 
      2015 Jan 31.