Evidence map›Paper›PMID 9514262›Full record

ArticleProtein science : a publication of the Protein Society1998

Structural analysis of the multienzyme aminoacyl-tRNA synthetase complex: a three-domain model based on reversible chemical crosslinking.

M T Norcum, J A Warrington

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020
    Review
  3. Article
  4. Article
  5. Aminoacyl-tRNA synthetase complexes in evolution.International journal of molecular sciences · 2015
    Review
  6. Article
  7. Architecture and metamorphosis.Topics in current chemistry · 2014
    Review
  8. Article
  9. Structural context for mobilization of a human tRNA synthetase from its cytoplasmic complex.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Chemistry for the analysis of protein-protein interactions: rapid and efficient cross-linking triggered by long wavelength light.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  16. Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  17. 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

2 authors at 1 institution in 1 country.

M T NorcumDepartment of Biochemistry, University of Mississippi Medical Center, Jackson 39216-4505, USA. mnorcum@fiona.umsmed.edu
J A Warrington
University of Mississippi Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A subset of eukaryotic aminoacyl-tRNA synthetases (a-RS) are contained in a multienzyme complex for which little structural detail is known. Three reversible chemical crosslinking reagents have been used to investigate the arrangement of polypeptides within this particle as isolated from rabbit reticulocytes. Identification of the crosslinked protein pairs was accomplished by two-dimensional SDS diagonal gel electrophoresis. Seventeen neighboring protein pairs have been identified. Eight are seen with at least two reagents: K-RS:p38, D-RS:K-RS, R-RS dimer, K-RS dimer, K-RS:Q-RS, E/P-RS:K-RS, E/P-RS:I-RS, and Q-RS with one of the nonsynthetase proteins. Nine more are observed with one reagent: D-RS dimer, R-RS:p43, D-RS:Q-RS, D-RS:M-RS, K-RS:L-RS, I-RS:R-RS, D-RS:E/P-RS, I-RS:Q-RS, I-RS:L-RS. One trimeric association is seen: E/P-RS:I-RS:L-RS. The observed neighboring protein pairs suggest that the polypeptides within the aminoacyl-tRNA synthetase complex are distributed in three structural domains of similar mass. These can be arranged in a U-shaped particle in which each "arm" is considered a domain and the third forms the "base" of the structure. The arms have been termed domain I (D-RS, M-RS, Q-RS) and domain II (K-RS, R-RS), with domain III (E/P-RS, I-RS, L-RS) assigned to the base. The smaller proteins (p38, p43) may bridge the domains. This proposed spatial relationship of these domains, as well as their compositions, are consistent with earlier studies. Thus, this study provides an initial three-dimensional working model of the arrangement of polypeptides within the multienzyme aminoacyl-tRNA synthetase complex.

Indexed as

Amino Acyl-tRNA SynthetasesAnimalsCisplatinCross-Linking ReagentsElectrophoresis, Polyacrylamide GelModels, MolecularPeptidesProtein ConformationRabbitsReticulocytesSuccinimides4-succinimidyloxycarbonyl-alpha-methyl-alpha(2-pyridyldithio)tolueneAmino Acyl-tRNA SynthetasesCisplatinCross-Linking Reagentsethylene glycolylbis(succinimidyl succinate)PeptidesSuccinimides

Identifiers

PMID9514262
PMCPMC2143804
OpenAlexW2110788185

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.