Evidence map›Paper›PMID 11118226›Full record

ArticleThe EMBO journal2000

A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation.

M Kaminska, M Deniziak, P Kerjan, J Barciszewski, M Mirande

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-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

28 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. A Moonlighting Human Protein Is Involved in Mitochondrial Import of tRNA.International journal of molecular sciences · 2015
    Article
  7. Article
  8. Article
  9. Architecture and metamorphosis.Topics in current chemistry · 2014
    Review
  10. Article
  11. Article
  12. Article
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  15. Article
  16. Article
  17. Review
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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

5 authors at 1 institution in 2 countries.

M KaminskaLaboratoire d'Enzymologie et Biochimie Structurales, CNRS, 1 Avenue de la Terrasse, 91190 Gif-sur-Yvette, France.
M Deniziak
P Kerjan
J Barciszewski
M Mirande
Laboratoire d'Enzymologie et Biochimie Structurales · FR

Funding

Investigation of metabolites related to manganese exposureF31ES027304 · NIEHS · UNIVERSITY OF WASHINGTON · PI BAKER, MARISSA GAYL · 2016 to 2017
$61k
NIEHS NIH HHS 27304C2054
6 · The paper itself

Abstract

The cDNA encoding rice methionyl-tRNA synthetase was isolated. The protein exhibited a C-terminal polypeptide appended to a classical MetRS domain. This supplementary domain is related to endothelial monocyte activating polypeptide II (EMAPII), a cytokine produced in mammals after cleavage of p43, a component of the multisynthetase complex. It is also related to Arc1p and Trbp111, two tRNA binding proteins. We expressed rice MetRS and a derivative with a deletion of its EMAPII-like domain. Band-shift analysis showed that this extra-domain provides MetRS with non-specific tRNA binding properties. The EMAPII-like domain contributed a 10-fold decrease in K:(M) for tRNA in the aminoacylation reaction catalyzed by the native enzyme, as compared with the C-terminally truncated MetRS. Consequently, the EMAPII domain provides MetRS with a better catalytic efficiency at the free tRNA concentration prevailing in vivo. This domain binds the acceptor minihelix of tRNA(Met) and facilitates its aminoacylation. These results suggest that the EMAPII module could be a relic of an ancient tRNA binding domain that was incorporated into primordial synthetases for aminoacylation of RNA minihelices taken as the ancestor of modern tRNA.

Indexed as

AcylationBase SequenceBinding SitesCloning, MolecularKineticsMethionine-tRNA LigaseMolecular Sequence DataNucleic Acid ConformationOryzaProtein Structure, QuaternaryRecombinant ProteinsRNA, Transfer, MetSequence DeletionMethionine-tRNA LigaseRecombinant ProteinsRNA, Transfer, Met

Identifiers

PMID11118226
PMCPMC305886
OpenAlexW2033495952

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.