Evidence map›Paper›PMID 12554667›Full record

ArticleThe EMBO journal2003

Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability.

Kirk Beebe, Lluis Ribas De Pouplana, Paul Schimmel

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

97 citing papers in PubMed, 162 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Frontiers in molecular biosciences · 2022
    Article
  15. Review
  16. Article
  17. A molecular link between cell wall biosynthesis, translation fidelity, and stringent response inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
  20. Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020
    Review

37 more citing papers are in PubMed but not listed here.

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.

Kirk BeebeThe Skaggs Institute for Chemical Biology, The Scripps Research Institute, Beckman Center, BCC379, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Lluis Ribas De Pouplana
Paul Schimmel
Scripps Research Institute · US

Funding

INVESTIGATIONS OF REACTIONS OF PHYSIOLOGICAL IMPORTANCER01GM015539 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHIMMEL, PAUL R · 1985 to 2011
$6.6M
GENETIC APPROACHES TO PROTEIN/NUCLEIC ACID INTERACTIONSR01GM023562 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHIMMEL, PAUL R · 1985 to 2012
$4.9M
REACTIONS OF PHYSIOLOGICAL IMPORTANCER37GM015539 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI SCHIMMEL, PAUL R · 1989 to 1998
–
NIGMS NIH HHS GM 15539NIGMS NIH HHS GM 23562NIGMS NIH HHS R01 GM015539
6 · The paper itself

Abstract

Editing of misactivated amino acids by class I tRNA synthetases is encoded by a specialized internal domain specific to class I enzymes. In contrast, little is known about editing activities of the structurally distinct class II enzymes. Here we show that the class II alanyl-tRNA synthetase (AlaRS) has a specialized internal domain that appears weakly related to an appended domain of threonyl-tRNA synthetase (ThrRS), but is unrelated to that found in class I enzymes. Editing of misactivated glycine or serine was shown to require a tRNA cofactor. Specific mutations in the aforementioned domain disrupt editing and lead to production of mischarged tRNA. This class-specific editing domain was found to be essential for cell growth, in the presence of elevated concentrations of glycine or serine. In contrast to ThrRS, where the editing domain is not found in all three kingdoms of living organisms, it was incorporated early into AlaRSs and is present throughout evolution. Thus, tRNA-dependent editing by AlaRS may have been critical for making the genetic code sufficiently accurate to generate the tree of life.

Indexed as

Cell SurvivalRNA EditingAdenosine TriphosphateAlanine-tRNA LigaseAmino Acid SequenceAnimalsEvolution, MolecularHumansModels, MolecularMolecular Sequence DataPhenotypePhylogenyPoint MutationProtein Structure, TertiaryRNA, TransferSequence AlignmentAdenosine TriphosphateAlanine-tRNA LigaseRNA, TransferThreonine-tRNA Ligase

Identifiers

PMID12554667
PMCPMC140749
OpenAlexW1980382519

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.