Evidence map›Paper›PMID 28977649›Full record

ArticleNucleic acids research2017

The RNA chaperone La promotes pre-tRNA maturation via indiscriminate binding of both native and misfolded targets.

Ana Vakiloroayaei, Neha S Shah, Marlene Oeffinger, Mark A Bayfield

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. The regulation, function and disease relevance of cytoplasmic tRNAs.Nature reviews. Molecular cell biology · 2026
    Review
  2. Optimized tRNA structure-seq reveals robust tRNA secondary structures inbioRxiv : the preprint server for biology · 2026
    Article
  3. Use of tRNA-Mediated Suppression to Assess RNA Chaperone Function.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. RNA modifying enzymes shape tRNA biogenesis and function.The Journal of biological chemistry · 2024
    Review
  9. Review
  10. Article
  11. Article
  12. Structure ofRNA biology · 2021
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Single-nucleotide control of tRNA folding cooperativity under near-cellular conditions.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Article
  20. Review
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

4 authors at 2 institutions in 1 country.

Ana VakiloroayaeiDepartment of Biology, York University, Toronto, Ontario M3J 1P3, Canada.
Neha S ShahDepartment of Biology, York University, Toronto, Ontario M3J 1P3, Canada.
Marlene OeffingerInstitut de Recherches Cliniques de Montréal (IRCM), 110 Avenue des Pins Ouest, Montréal, Québec H2W 1R7, Canada.
Mark A BayfieldDepartment of Biology, York University, Toronto, Ontario M3J 1P3, Canada.
York University · CAMontreal Clinical Research Institute · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Non-coding RNAs have critical roles in biological processes, and RNA chaperones can promote their folding into the native shape required for their function. La proteins are a class of highly abundant RNA chaperones that contact pre-tRNAs and other RNA polymerase III transcripts via their common UUU-3'OH ends, as well as through less specific contacts associated with RNA chaperone activity. However, whether La proteins preferentially bind misfolded pre-tRNAs or instead engage all pre-tRNA substrates irrespective of their folding status is not known. La deletion in yeast is synthetically lethal when combined with the loss of tRNA modifications predicted to contribute to the native pre-tRNA fold, such as the N2, N2-dimethylation of G26 by the methyltransferase Trm1p. In this work, we identify G26 containing pre-tRNAs that misfold in the absence of Trm1p and/or La (Sla1p) in Schizosaccharomyces pombe cells, then test whether La preferentially associates with such tRNAs in vitro and in vivo. Our data suggest that La does not discriminate a native from misfolded RNA target, and highlights the potential challenges faced by RNA chaperones in preferentially binding defective substrates.

Indexed as

Models, GeneticModels, MolecularMutationProtein BindingRNA-Binding ProteinsRNA FoldingRNA PrecursorsRNA Processing, Post-TranscriptionalRNA, TransferSchizosaccharomycesSchizosaccharomyces pombe ProteinsRNA-Binding ProteinsRNA PrecursorsRNA, TransferSchizosaccharomyces pombe Proteinssla1 protein, S pombe

Identifiers

PMID28977649
PMCPMC5737608
OpenAlexW2753678251

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.