ArticleNucleic acids research2018
Unstructured 5'-tails act through ribosome standby to override inhibitory structure at ribosome binding sites.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 36 citations in OpenAlex.
- An RNA structural switch controlling bacterial toxin translation.Nucleic acids research · 2026Article
- ProQ-associated small RNAs control motility in Vibrio cholerae.Nucleic acids research · 2025Article
- A simple BLASTn-based approach generates novel insights into the regulation and biological function of type I toxin-antitoxins.mSystems · 2024Article
- 5' Untranslated mRNA Regions Allow Bypass of Host Cell Translation Inhibition by Legionella pneumophila.Infection and immunity · 2022Article
- Translation initiation site of mRNA is selected through dynamic interaction with the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Research progress of pathway and genome evolution in microbes.Synthetic and systems biotechnology · 2022Article
- The diversity of Shine-Dalgarno sequences sheds light on the evolution of translation initiation.RNA biology · 2021Review
- Importance of the 5' regulatory region to bacterial synthetic biology applications.Microbial biotechnology · 2021Review
- Switching at the ribosome: riboswitches need rProteins as modulators to regulate translation.Nature communications · 2021Article
- An RNA pseudoknot is essential for standby-mediated translation of the tisB toxin mRNA in Escherichia coli.Nucleic acids research · 2020Article
- Translation inhibition from a distance: The small RNA SgrS silences a ribosomal protein S1-dependent enhancer.Molecular microbiology · 2020Article
- Autogenous regulation in vivo of theRNA (New York, N.Y.) · 2020Article
- The Impact of Leadered and Leaderless Gene Structures on Translation Efficiency, Transcript Stability, and Predicted Transcription Rates in Mycobacterium smegmatis.Journal of bacteriology · 2020Article
- Review
- Recent advances in genetic engineering tools based on synthetic biology.Journal of microbiology (Seoul, Korea) · 2020Review
- The ribosomal protein S1-dependent standby site inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Type I Toxin-Antitoxin Systems: Regulating Toxin Expression via Shine-Dalgarno Sequence Sequestration and Small RNA Binding.Microbiology spectrum · 2018Review
- Translation initiation in bacterial polysomes through ribosome loading on a standby site on a highly translated mRNA.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
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
Initiation is the rate-limiting step in translation. It is well-known that stable structure at a ribosome binding site (RBS) impedes initiation. The ribosome standby model of de Smit and van Duin, based on studies of the MS2 phage coat cistron, proposed how high translation rates can be reconciled with stable, inhibitory structures at an RBS. Here, we revisited the coat protein system and assessed the translation efficiency from its sequestered RBS by introducing standby mutations. Further experiments with gfp reporter constructs assessed the effects of 5'-tails-as standby sites-with respect to length and sequence contributions. In particular, combining in vivo and in vitro assays, we can show that tails of CA-dinucleotide repeats-and to a lesser extent, AU-repeats-dramatically increase translation rates. Tails of increasing length reach maximal rate-enhancing effects at 16-18 nucleotides. These standby tails are single-stranded and do not exert their effect by structure changes in the neighboring RBS stem-loop. In vitro translation and toeprinting assays furthermore demonstrate that standby effects are exerted at the level of translation initiation. Finally, as expected, destabilizing mutations within the coat RBS indicate an interplay with the effects of standby tails.
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.