Evidence map›Paper›PMID 25959893›Full record

ReviewWiley interdisciplinary reviews. RNA

Structure and mechanism of the T-box riboswitches.

Jinwei Zhang, Adrian R Ferré-D'Amaré

Open access · greenAbstract readReview
In one paragraph

Review in Wiley interdisciplinary reviews. RNA. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The current riboswitch landscape inMicrobiology (Reading, England) · 2024
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. A Riboswitch-Driven Era of New Antibacterials.Antibiotics (Basel, Switzerland) · 2022
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Improving RNA Crystal Diffraction Quality by Postcrystallization Treatment.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Jinwei ZhangBiochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, Bethesda, MD, USA.
Adrian R Ferré-D'AmaréBiochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, Bethesda, MD, USA.
National Heart Lung and Blood Institute · US

Funding

RNA: Structure, Biophysics and PhysiologyZIAHL006102 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI FERRÉ-D'AMARÉ, ADRIAN · 2011 to 2025
$14.6M
Intramural NIH HHS ZIA HL006102
6 · The paper itself

Abstract

In most Gram-positive bacteria, including many clinically devastating pathogens from genera such as Bacillus, Clostridium, Listeria, and Staphylococcus, T-box riboswitches sense and regulate intracellular availability of amino acids through a multipartite messenger RNA (mRNA)-transfer RNA (tRNA) interaction. The T-box mRNA leaders respond to nutrient starvation by specifically binding cognate tRNAs and sensing whether the bound tRNA is aminoacylated, as a proxy for amino acid availability. Based on this readout, T-boxes direct a transcriptional or translational switch to control the expression of downstream genes involved in various aspects of amino acid metabolism: biosynthesis, transport, aminoacylation, transamidation, and so forth. Two decades after its discovery, the structural and mechanistic underpinnings of the T-box riboswitch were recently elucidated, producing a wealth of insights into how two structured RNAs can recognize each other with robust affinity and exquisite selectivity. The T-box paradigm exemplifies how natural noncoding RNAs can interact not just through sequence complementarity but can add molecular specificity by precisely juxtaposing RNA structural motifs, exploiting inherently flexible elements and the biophysical properties of post-transcriptional modifications, ultimately achieving a high degree of shape complementarity through mutually induced fit. The T-box also provides a proof-of-principle that compact RNA domains can recognize minute chemical changes (such as tRNA aminoacylation) on another RNA. The unveiling of the structure and mechanism of the T-box system thus expands our appreciation of the range of capabilities and modes of action of structured noncoding RNAs, and hints at the existence of networks of noncoding RNAs that communicate through both, structural and sequence specificity.

Indexed as

RiboswitchRNA, TransferT-Box Domain ProteinsRNA Processing, Post-TranscriptionalRiboswitchRNA, TransferT-Box Domain Proteins

Identifiers

PMID25959893
PMCPMC4478136
OpenAlexW1596520289

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.