ArticleRNA (New York, N.Y.)2014
An unusual mechanism for EF-Tu activation during tmRNA-mediated ribosome rescue.
Article in RNA (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 22 citations in OpenAlex.
- AJournal of bacteriology · 2025Article
- Article
- The Structural and Molecular Mechanisms ofMolecules (Basel, Switzerland) · 2024Review
- Endogenous trans-translation structure visualizes the decoding of the first tmRNA alanine codon.Frontiers in microbiology · 2024Article
- Druggable differences: Targeting mechanistic differences between trans-translation and translation for selective antibiotic action.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022Article
- Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021Review
- How a circularized tmRNA moves through the ribosome.Science (New York, N.Y.) · 2019Article
- Elfamycins: inhibitors of elongation factor-Tu.Molecular microbiology · 2017Review
- Mechanisms of ribosome rescue in bacteria.Nature reviews. Microbiology · 2015Review
- The bacterial translation stress response.FEMS microbiology reviews · 2014Review
- Rejection of tmRNA·SmpB after GTP hydrolysis by EF-Tu on ribosomes stalled on intact mRNA.RNA (New York, N.Y.) · 2014Article
- tmRNA-mediated trans-translation as the major ribosome rescue system in a bacterial cell.Frontiers in genetics · 2014Review
- Trans-translation exposed: understanding the structures and functions of tmRNA-SmpB.Frontiers in microbiology · 2014Review
- Mechanism of trans-translation revealed by in vitro studies.Frontiers in microbiology · 2014Review
- The SmpB C-terminal tail helps tmRNA to recognize and enter stalled ribosomes.Frontiers in microbiology · 2014Review
- Ends of the line for tmRNA-SmpB.Frontiers in microbiology · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In bacteria, ribosomes stalled on truncated mRNAs are rescued by transfer-messenger RNA (tmRNA) and its protein partner SmpB. Acting like tRNA, the aminoacyl-tmRNA/SmpB complex is delivered to the ribosomal A site by EF-Tu and accepts the transfer of the nascent polypeptide. Although SmpB binding within the decoding center is clearly critical for licensing tmRNA entry into the ribosome, it is not known how activation of EF-Tu occurs in the absence of a codon-anticodon interaction. A recent crystal structure revealed that SmpB residue His136 stacks on 16S rRNA nucleotide G530, a critical player in the canonical decoding mechanism. Here we use pre-steady-state kinetic methods to probe the role of this interaction in ribosome rescue. We find that although mutation of His136 does not reduce SmpB's affinity for the ribosomal A-site, it dramatically reduces the rate of GTP hydrolysis by EF-Tu. Surprisingly, the same mutation has little effect on the apparent rate of peptide-bond formation, suggesting that release of EF-Tu from the tmRNA/SmpB complex on the ribosome may occur prior to GTP hydrolysis. Consistent with this idea, we find that peptidyl transfer to tmRNA is relatively insensitive to the antibiotic kirromycin. Taken together, our studies provide a model for the initial stages of ribosomal rescue by tmRNA.
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.