Evidence map›Paper›PMID 21518804›Full record

ArticleRNA (New York, N.Y.)2011

A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop.

Sonia D'Silva, Steffen J Haider, Eric M Phizicky

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

51 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Structural basis of tRNA recognition by the mNature structural & molecular biology · 2024
    Article
  3. Article
  4. Review
  5. mNature communications · 2024
    Article
  6. Article
  7. Human TRMT1 catalyzes mScience China. Life sciences · 2023
    Article
  8. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  9. Article
  10. Article
  11. Article
  12. The RNA methyltransferase METTL8 installs mNature communications · 2022
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. METTL6 is a tRNA mScience advances · 2020
    Article
  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

3 authors at 1 institution in 1 country.

Sonia D'SilvaDepartment of Biochemistry and Biophysics and Center for RNA Biology, University of Rochester School of Medicine, Rochester, New York 14642, USA.
Steffen J Haider
Eric M Phizicky
University of Rochester · US

Funding

TRNA SPLICINGR01GM052347 · NIGMS · UNIVERSITY OF ROCHESTER · PI Eric M. Phizicky · 1995 to 2026
$9.6M
NIGMS NIH HHS GM52347NIGMS NIH HHS R01 GM052347
6 · The paper itself

Abstract

The 3-methylcytidine (m³C) modification is widely found in eukaryotic species of tRNA(Ser), tRNA(Thr), and tRNA(Arg); at residue 32 in the anti-codon loop; and at residue e2 in the variable stem of tRNA(Ser). Little is known about the function of this modification or about the specificity of the corresponding methyltransferase, since the gene has not been identified. We have used a primer extension assay to screen a battery of methyltransferase candidate knockout strains in the yeast Saccharomyces cerevisiae, and find that tRNA(Thr(IGU)) from abp140-Δ strains lacks m³C. Curiously, Abp140p is composed of a poorly conserved N-terminal ORF fused by a programed +1 frameshift in budding yeasts to a C-terminal ORF containing an S-adenosylmethionine (SAM) domain that is highly conserved among eukaryotes. We show that ABP140 is required for m³C modification of substrate tRNAs, since primer extension is similarly affected for all tRNA species expected to have m³C and since quantitative analysis shows explicitly that tRNA(Thr(IGU)) from an abp140-Δ strain lacks m³C. We also show that Abp140p (now named Trm140p) purified after expression in yeast or Escherichia coli has m³C methyltransferase activity, which is specific for tRNA(Thr(IGU)) and not tRNA(Phe) and occurs specifically at C₃₂. We suggest that the C-terminal ORF of Trm140p is necessary and sufficient for activity in vivo and in vitro, based on analysis of constructs deleted for most or all of the N-terminal ORF. We also suggest that m³C has a role in translation, since trm140-Δ trm1-Δ strains (also lacking m²,²G₂₆) are sensitive to low concentrations of cycloheximide.

Indexed as

AnticodonCytidineMicrofilament ProteinsNucleic Acid ConformationProtein Structure, TertiaryRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsS-AdenosylmethioninetRNA Methyltransferases3-methylcytidineABP140 protein, S cerevisiaeAnticodonCytidineMicrofilament ProteinsRNA, TransferSaccharomyces cerevisiae ProteinsS-AdenosylmethioninetRNA Methyltransferases

Identifiers

PMID21518804
PMCPMC3096042
OpenAlexW2097843864

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.