Evidence map›Paper›PMID 17766929›Full record

ArticleNucleic acids research2007

An aminoacyl-tRNA synthetase:elongation factor complex for substrate channeling in archaeal translation.

Corinne D Hausmann, Mette Praetorius-Ibba, Michael Ibba

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Aminoacyl-tRNA synthetase complexes in evolution.International journal of molecular sciences · 2015
    Review
  6. Structure of the Pseudomonas aeruginosa transamidosome reveals unique aspects of bacterial tRNA-dependent asparagine biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  7. Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Exit strategies for charged tRNA from GluRS.Journal of molecular biology · 2010
    Article
  15. Article
  16. Review
  17. Article
  18. tRNA synthetase: tRNA aminoacylation and beyond.Wiley interdisciplinary reviews. RNA
    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

3 authors at 1 institution in 1 country.

Corinne D HausmannDepartment of Microbiology, Ohio State Biochemistry Program, and Ohio State RNA Group, The Ohio State University, Columbus, Ohio 43210-1292, USA.
Mette Praetorius-Ibba
Michael Ibba
The Ohio State University · US

Funding

Mechanisms of translational controlR01GM065183 · NIGMS · OHIO STATE UNIVERSITY · PI DUNHAM, CHRISTINE M, FREDRICK, KURT L · 2003 to 2020
$4.9M
NIGMS NIH HHS GM 65183NIGMS NIH HHS R01 GM065183
6 · The paper itself

Abstract

Translation requires the specific attachment of amino acids to tRNAs by aminoacyl-tRNA synthetases (aaRSs) and the subsequent delivery of aminoacyl-tRNAs to the ribosome by elongation factor 1 alpha (EF-1alpha). Interactions between EF-1alpha and various aaRSs have been described in eukaryotes, but the role of these complexes remains unclear. To investigate possible interactions between EF-1alpha and other cellular components, a yeast two-hybrid screen was performed for the archaeon Methanothermobacter thermautotrophicus. EF-1alpha was found to form a stable complex with leucyl-tRNA synthetase (LeuRS; K(D) = 0.7 microM). Complex formation had little effect on EF-1alpha activity, but increased the k(cat) for Leu-tRNA(Leu) synthesis approximately 8-fold. In addition, EF-1alpha co-purified with the archaeal multi-synthetase complex (MSC) comprised of LeuRS, LysRS and ProRS, suggesting the existence of a larger aaRS:EF-1alpha complex in archaea. These interactions between EF-1alpha and the archaeal MSC contribute to translational fidelity both by enhancing the aminoacylation efficiencies of the three aaRSs in the complex and by coupling two stages of translation: aminoacylation of cognate tRNAs and their subsequent channeling to the ribosome.

Indexed as

Transfer RNA AminoacylationAlanine-tRNA LigaseAmino Acyl-tRNA SynthetasesArchaeal ProteinsGuanosine TriphosphateLeucine-tRNA LigaseMethanobacteriaceaePeptide Elongation Factor 1Protein BiosynthesisTwo-Hybrid System TechniquesAlanine-tRNA LigaseAmino Acyl-tRNA SynthetasesArchaeal ProteinsGuanosine TriphosphateLeucine-tRNA LigasePeptide Elongation Factor 1

Identifiers

PMID17766929
PMCPMC2094089
OpenAlexW2031720204

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.