Evidence map›Paper›PMID 25918939›Full record

ArticleInternational journal of molecular sciences2015

A Moonlighting Human Protein Is Involved in Mitochondrial Import of tRNA.

Maria Baleva, Ali Gowher, Piotr Kamenski, Ivan Tarassov, Nina Entelis, Benoît Masquida

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

9 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  7. When Place Matters: Shuttling of Enolase-1 Across Cellular Compartments.Frontiers in cell and developmental biology · 2019
    Review
  8. 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

6 authors at 2 institutions in 2 countries.

Maria BalevaDepartment of Molecular and Cellular Genetics, UMR 7156 Génétique Moléculaire, Génomique, Microbiologie (GMGM), CNRS-Université de Strasbourg, 67084 Strasbourg, France. piotr.kamenski@gmail.com.
Ali GowherDepartment of Molecular and Cellular Genetics, UMR 7156 Génétique Moléculaire, Génomique, Microbiologie (GMGM), CNRS-Université de Strasbourg, 67084 Strasbourg, France. qureishi83@gmail.com.
Piotr KamenskiDepartment of Molecular Biology, Biology Faculty of Moscow State University, 119992 Moscow, Russia. piotr.kamenski@gmail.com.
Ivan TarassovDepartment of Molecular and Cellular Genetics, UMR 7156 Génétique Moléculaire, Génomique, Microbiologie (GMGM), CNRS-Université de Strasbourg, 67084 Strasbourg, France. i.tarassov@unistra.fr.
Nina EntelisDepartment of Molecular and Cellular Genetics, UMR 7156 Génétique Moléculaire, Génomique, Microbiologie (GMGM), CNRS-Université de Strasbourg, 67084 Strasbourg, France. n.entelis@unistra.fr.
Benoît MasquidaDepartment of Molecular and Cellular Genetics, UMR 7156 Génétique Moléculaire, Génomique, Microbiologie (GMGM), CNRS-Université de Strasbourg, 67084 Strasbourg, France. b.masquida@unistra.fr.
Centre National de la Recherche Scientifique · FRLomonosov Moscow State University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In yeast Saccharomyces cerevisiae, ~3% of the lysine transfer RNA acceptor 1 (tRK1) pool is imported into mitochondria while the second isoacceptor, tRK2, fully remains in the cytosol. The mitochondrial function of tRK1 is suggested to boost mitochondrial translation under stress conditions. Strikingly, yeast tRK1 can also be imported into human mitochondria in vivo, and can thus be potentially used as a vector to address RNAs with therapeutic anti-replicative capacity into mitochondria of sick cells. Better understanding of the targeting mechanism in yeast and human is thus critical. Mitochondrial import of tRK1 in yeast proceeds first through a drastic conformational rearrangement of tRK1 induced by enolase 2, which carries this freight to the mitochondrial pre-lysyl-tRNA synthetase (preMSK). The latter may cross the mitochondrial membranes to reach the matrix where imported tRK1 could be used by the mitochondrial translation apparatus. This work focuses on the characterization of the complex that tRK1 forms with human enolases and their role on the interaction between tRK1 and human pre-lysyl-tRNA synthetase (preKARS2).

Indexed as

AlgorithmsAmino Acid SequenceBase SequenceBiological TransportCation Transport ProteinsCytosolDatabases, ProteinHep G2 CellsHumansLysine-tRNA LigaseMitochondriaModels, MolecularMolecular Sequence DataNucleic Acid ConformationPhosphopyruvate HydrataseProtein BiosynthesisCation Transport ProteinsLysine-tRNA LigasePhosphopyruvate HydrataseRNA, TransferSaccharomyces cerevisiae ProteinsTRK1 protein, S cerevisiae

Identifiers

PMID25918939
PMCPMC4463592
OpenAlexW2159701569

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.