Evidence map›Paper›PMID 18522806›Full record

ReviewBiochimica et biophysica acta2009

Roles of Oxa1-related inner-membrane translocases in assembly of respiratory chain complexes.

Nathalie Bonnefoy, Heather L Fiumera, Geneviève Dujardin, Thomas D Fox

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

43 citing papers in PubMed, 86 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. A Role forMicroorganisms · 2019
    Article
  11. Review
  12. Article
  13. Article
  14. Building the CuThe Journal of biological chemistry · 2018
    Review
  15. Human mitochondrial cytochromeThe Journal of biological chemistry · 2017
    Article
  16. Article
  17. Article
  18. YidC/Alb3/Oxa1 Family of Insertases.The Journal of biological chemistry · 2015
    Review
  19. Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015
    Review
  20. Article
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

4 authors at 2 institutions in 2 countries.

Nathalie BonnefoyCentre de Génétique Moléculaire, CNRS UPR 2167, Avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex, France.
Heather L Fiumera
Geneviève Dujardin
Thomas D Fox
Centre National de la Recherche Scientifique · FRCornell University · US

Funding

TRANSLATIONAL CONTROL OF YEAST MITOCHONDRIAL GENESR01GM029362 · NIGMS · CORNELL UNIVERSITY ITHACA · PI FOX, THOMAS DAVID · 1985 to 2013
$6.1M
NIGMS NIH HHS GM29362NIGMS NIH HHS R01 GM029362
6 · The paper itself

Abstract

Members of the family of the polytopic inner membrane proteins are related to Saccharomyces cerevisiae Oxa1 function in the assembly of energy transducing complexes of mitochondria and chloroplasts. Here we focus on the two mitochondrial members of this family, Oxa1 and Cox18, reviewing studies on their biogenesis as well as their functions, reflected in the phenotypic consequences of their absence in various organisms. In yeast, cytochrome c oxidase subunit II (Cox2) is a key substrate of these proteins. Oxa1 is required for co-translational translocation and insertion of Cox2, while Cox18 is necessary for the export of its C-terminal domain. Genetic and biochemical strategies have been used to investigate the functions of distinct domains of Oxa1 and to identify its partners in protein insertion/translocation. Recent work on the related bacterial protein YidC strongly indicates that it is capable of functioning alone as a translocase for hydrophilic domains and an insertase for TM domains. Thus, the Oxa1 and Cox18 probably catalyze these reactions directly in a co- and/or posttranslational way. In various species, Oxa1 appears to assist in the assembly of different substrate proteins, although it is still unclear how Oxa1 recognizes its substrates, and whether additional factors participate in this beyond its direct interaction with mitochondrial ribosomes, demonstrated in S. cerevisiae. Oxa1 is capable of assisting posttranslational insertion and translocation in isolated mitochondria, and Cox18 may posttranslationally translocate its only known substrate, the Cox2 C-terminal domain, in vivo. Detailed understanding of the mechanisms of action of these two proteins must await the resolution of their structure in the membrane and the development of a true in vitro mitochondrial translation system.

Indexed as

Amino Acid SequenceAnimalsElectron TransportElectron Transport Chain Complex ProteinsElectron Transport Complex IVEscherichia coliEvolution, MolecularHumansMembrane Transport ProteinsMitochondrial MembranesMitochondrial ProteinsNuclear ProteinsSaccharomyces cerevisiaeElectron Transport Chain Complex ProteinsElectron Transport Complex IVMembrane Transport ProteinsMitochondrial ProteinsNuclear ProteinsOXA1 protein

Identifiers

PMID18522806
PMCPMC2658530
OpenAlexW2123774841

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.