Evidence map›Paper›PMID 26063805›Full record

ArticleThe Journal of biological chemistry2015

The Levels of a Universally Conserved tRNA Modification Regulate Cell Growth.

Diego Rojas-Benitez, Patrick C Thiaville, Valérie de Crécy-Lagard, Alvaro Glavic

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 37 citations in OpenAlex.

  1. Catalytic and regulatory basis of tRNA tNature communications · 2026
    Article
  2. Article
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  7. Article
  8. Article
  9. Review
  10. Review
  11. Loss ofeLife · 2021
    Article
  12. Article
  13. Review
  14. Naturally occurring modified ribonucleosides.Wiley interdisciplinary reviews. RNA · 2020
    Review
  15. Article
  16. Elongator Subunit 3 (Elp3) Is Required for Zebrafish Trunk Development.International journal of molecular sciences · 2020
    Article
  17. Frontiers in microbiology · 2019
    Article
  18. Article
  19. Article
  20. The tRNA biology · 2018
    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

4 authors at 2 institutions in 2 countries.

Diego Rojas-BenitezFrom the Centro de Regulación del Genoma, Facultad de Ciencias, Universidad de Chile, Las Palmeras 3425, Santiago, Chile 7800024 and.
Patrick C Thiavillethe Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida32611-0700.
Valérie de Crécy-Lagardthe Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida32611-0700.ORCID http://orcid.org/0000-0002-9955-3785
Alvaro GlavicFrom the Centro de Regulación del Genoma, Facultad de Ciencias, Universidad de Chile, Las Palmeras 3425, Santiago, Chile 7800024 and alglavic@uchile.cl.
University of Chile · CLUniversity of Florida · US

Funding

Resource Component: Acquisition, maintenance and distribution of Drosophila stocksP40OD018537 · OD · TRUSTEES OF INDIANA UNIVERSITY · PI Annette L. Parks · 2014 to 2026
$13.5M
Synthesis and function of Queuosine in BacteriaR01GM070641 · NIGMS · UNIVERSITY OF FLORIDA · PI DE CRECY-LAGARD, VALERIE A · 2006 to 2023
$5.3M
NIGMS NIH HHS R01 GM070641NIGMS NIH HHS R01 GM70641NIH HHS P40 OD018537NIH HHS P40OD018537
6 · The paper itself

Abstract

N(6)-Threonylcarbamoyl-adenosine (t(6)A) is a universal modification occurring at position 37 in nearly all tRNAs that decode A-starting codons, including the eukaryotic initiator tRNA (tRNAi (Met)). Yeast lacking central components of the t(6)A synthesis machinery, such as Tcs3p (Kae1p) or Tcs5p (Bud32p), show slow-growth phenotypes. In the present work, we show that loss of the Drosophila tcs3 homolog also leads to a severe reduction in size and demonstrate, for the first time in a non-microbe, that Tcs3 is required for t(6)A synthesis. In Drosophila and in mammals, tRNAi (Met) is a limiting factor for cell and animal growth. We report that the t(6)A-modified form of tRNAi (Met) is the actual limiting factor. We show that changing the proportion of t(6)A-modified tRNAi (Met), by expression of an un-modifiable tRNAi (Met) or changing the levels of Tcs3, regulate target of rapamycin (TOR) kinase activity and influences cell and animal growth in vivo. These findings reveal an unprecedented relationship between the translation machinery and TOR, where translation efficiency, limited by the availability of t(6)A-modified tRNA, determines growth potential in eukaryotic cells.

Indexed as

AnimalsCell ProliferationCodon, InitiatorDrosophilaGene Expression RegulationProtein BiosynthesisProtein Serine-Threonine KinasesRNA Processing, Post-TranscriptionalRNA, Transfer, MetSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTOR Serine-Threonine KinasesVesicular Transport ProteinsBUD32 protein, S cerevisiaeCodon, InitiatorProtein Serine-Threonine KinasesRNA, Transfer, MetSaccharomyces cerevisiae ProteinsTOR Serine-Threonine KinasesVesicular Transport ProteinsVPS54 protein, S cerevisiaecell growthDrosophilatransfer RNA (tRNA)translationyeast

Identifiers

PMID26063805
PMCPMC4513126
OpenAlexW2199441322

What OpenQuestion holds

Textmetadata
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.