Evidence map›Paper›PMID 25114051›Full record

ArticleNucleic acids research2014

Molecular basis for the differential interaction of plant mitochondrial VDAC proteins with tRNAs.

Thalia Salinas, Samira El Farouk-Ameqrane, Elodie Ubrig, Claude Sauter, Anne-Marie Duchêne, Laurence Maréchal-Drouard

Erratum issuedAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Cells · 2020
    Article
  10. Review
  11. Article
  12. tRNAs and proteins use the same import channel for translocation across the mitochondrial outer membrane of trypanosomes.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  13. Review
  14. tRNA biology in mitochondria.International journal of molecular sciences · 2015
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Thalia SalinasInstitut de Biologie Moléculaire des Plantes, UPR 2357 CNRS, associated with Strasbourg University, 12 rue du Général Zimmer 67084 Strasbourg cedex, France laurence.drouard@ibmp-cnrs.unistra.fr.
Samira El Farouk-AmeqraneInstitut de Biologie Moléculaire des Plantes, UPR 2357 CNRS, associated with Strasbourg University, 12 rue du Général Zimmer 67084 Strasbourg cedex, France.
Elodie UbrigInstitut de Biologie Moléculaire des Plantes, UPR 2357 CNRS, associated with Strasbourg University, 12 rue du Général Zimmer 67084 Strasbourg cedex, France.
Claude SauterInstitut de Biologie Moléculaire et Cellulaire, UPR 9002 CNRS, associated with Strasbourg University, 15 rue René Descartes 67084 Strasbourg cedex, France.
Anne-Marie DuchêneInstitut de Biologie Moléculaire des Plantes, UPR 2357 CNRS, associated with Strasbourg University, 12 rue du Général Zimmer 67084 Strasbourg cedex, France.
Laurence Maréchal-DrouardInstitut de Biologie Moléculaire des Plantes, UPR 2357 CNRS, associated with Strasbourg University, 12 rue du Général Zimmer 67084 Strasbourg cedex, France laurence.drouard@ibmp-cnrs.unistra.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plants, the voltage-dependent anion-selective channel (VDAC) is a major component of a pathway involved in transfer RNA (tRNA) translocation through the mitochondrial outer membrane. However, the way in which VDAC proteins interact with tRNAs is still unknown. Potato mitochondria contain two major mitochondrial VDAC proteins, VDAC34 and VDAC36. These two proteins, composed of a N-terminal α-helix and of 19 β-strands forming a β-barrel structure, share 75% sequence identity. Here, using both northwestern and gel shift experiments, we report that these two proteins interact differentially with nucleic acids. VDAC34 binds more efficiently with tRNAs or other nucleic acids than VDAC36. To further identify specific features and critical amino acids required for tRNA binding, 21 VDAC34 mutants were constructed and analyzed by northwestern. This allowed us to show that the β-barrel structure of VDAC34 and the first 50 amino acids that contain the α-helix are essential for RNA binding. Altogether the work shows that during evolution, plant mitochondrial VDAC proteins have diverged so as to interact differentially with nucleic acids, and this may reflect their involvement in various specialized biological functions.

Indexed as

DNA, PlantMitochondrial ProteinsModels, MolecularPlant ProteinsProtein BindingProtein IsoformsRNA, PlantRNA, TransferSolanum tuberosumVoltage-Dependent Anion ChannelsDNA, PlantMitochondrial ProteinsPlant ProteinsProtein IsoformsRNA, PlantRNA, TransferVoltage-Dependent Anion Channels

Identifiers

PMID25114051
PMCPMC4150812

What OpenQuestion holds

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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.