ArticleJournal of bacteriology2007
Ribosome recycling factor and release factor 3 action promotes TnaC-peptidyl-tRNA Dropoff and relieves ribosome stalling during tryptophan induction of tna operon expression in Escherichia coli.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- Translation quality control in Pseudomonas aeruginosa: current knowledge and perspectives.FEMS microbiology reviews · 2026Review
- Quality control of protein synthesis in the early elongation stage.Nature communications · 2023Article
- Drop-off-reinitiation at the amino termini of nascent peptides and its regulation by IF3, EF-G, and RRF.RNA (New York, N.Y.) · 2023Article
- Drop-off-reinitiation triggered by EF-G-driven mistranslocation and its alleviation by EF-P.Nucleic acids research · 2022Article
- Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021Review
- Conserved Upstream Open Reading Frame Nascent Peptides That Control Translation.Annual review of genetics · 2020Review
- Interactions of release factor RF3 with the translation machinery.Molecular genetics and genomics : MGG · 2015Article
- Mechanism of trans-translation revealed by in vitro studies.Frontiers in microbiology · 2014Review
- tmRNA-mediated trans-translation as the major ribosome rescue system in a bacterial cell.Frontiers in genetics · 2014Review
- Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB8.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Structural basis for the substrate recognition and catalysis of peptidyl-tRNA hydrolase.Nucleic acids research · 2012Article
- The tmRNA ribosome-rescue system.Advances in protein chemistry and structural biology · 2012Review
- Alternative fates of paused ribosomes during translation termination.The Journal of biological chemistry · 2011Article
- Functional significance of an evolutionarily conserved alanine (GCA) resume codon in tmRNA in Escherichia coli.Journal of bacteriology · 2011Article
- Termination and antitermination: RNA polymerase runs a stop sign.Nature reviews. Microbiology · 2011Review
- Kinetics of paused ribosome recycling in Escherichia coli.Journal of molecular biology · 2009Article
- A new view of protein synthesis: mapping the free energy landscape of the ribosome using single-molecule FRET.Biopolymers · 2008Review
- The ribosome: a metabolite-responsive transcription regulator.Journal of bacteriology · 2008Review
- Complementary roles of initiation factor 1 and ribosome recycling factor in 70S ribosome splitting.The EMBO journal · 2008Article
- Modulating the activity of the peptidyl transferase center of the ribosome.RNA (New York, N.Y.) · 2008Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Upon tryptophan induction of tna operon expression in Escherichia coli, the leader peptidyl-tRNA, TnaC-tRNA(2)(Pro), resists cleavage, resulting in ribosome stalling at the tnaC stop codon. This stalled ribosome blocks Rho factor binding and action, preventing transcription termination in the tna operon's leader region. Plasmid-mediated overexpression of tnaC was previously shown to inhibit cell growth by reducing uncharged tRNA(2)(Pro) availability. Which factors relieve ribosome stalling, facilitate TnaC-tRNA(2)(Pro) cleavage, and relieve growth inhibition were addressed in the current study. In strains containing the chromosomal tna operon and lacking a tnaC plasmid, the overproduction of ribosome recycling factor (RRF) and release factor 3 (RF3) reduced tna operon expression. Their overproduction in vivo also increased the rate of cleavage of TnaC-tRNA(2)(Pro), relieving the growth inhibition associated with plasmid-mediated tnaC overexpression. The overproduction of elongation factor G or initiation factor 3 did not have comparable effects, and tmRNA was incapable of attacking TnaC-tRNA(2)(Pro) in stalled ribosome complexes. The stability of TnaC-tRNA(2)(Pro) was increased appreciably in strains deficient in RRF and RF3 or deficient in peptidyl-tRNA hydrolase. These findings reveal the existence of a natural mechanism whereby an amino acid, tryptophan, binds to ribosomes that have just completed the synthesis of TnaC-tRNA(2)(Pro). Bound tryptophan inhibits RF2-mediated cleavage of TnaC-tRNA(2)(Pro), resulting in the stalling of the ribosome translating tnaC mRNA. This stalling results in increased transcription of the structural genes of the tna operon. RRF and RF3 then bind to this stalled ribosome complex and slowly release TnaC-tRNA(2)(Pro). This release allows ribosome recycling and permits the cleavage of TnaC-tRNA(2)(Pro) by peptidyl-tRNA hydrolase.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.