Evidence map›Paper›PMID 17452441›Full record

ArticleMolecular and cellular biology2007

Translocation of mitochondrially synthesized Cox2 domains from the matrix to the intermembrane space.

Heather L Fiumera, Sarah A Broadley, Thomas D Fox

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Functions of CytochromeInternational journal of molecular sciences · 2020
    Review
  7. Article
  8. Article
  9. Building the CuThe Journal of biological chemistry · 2018
    Review
  10. Plant Mitochondrial Inner Membrane Protein Insertion.International journal of molecular sciences · 2018
    Review
  11. The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis.Biochimica et biophysica acta. Molecular cell research · 2018
    Article
  12. Article
  13. Human mitochondrial cytochromeThe Journal of biological chemistry · 2017
    Article
  14. Article
  15. YidC/Alb3/Oxa1 Family of Insertases.The Journal of biological chemistry · 2015
    Review
  16. Article
  17. Review
  18. Article
  19. A single mutation in the first transmembrane domain of yeast COX2 enables its allotopic expression.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  20. 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

3 authors at 1 institution in 1 country.

Heather L FiumeraDepartment of Molecular Biology and Genetics, Biotechnology Building, Cornell University, Ithaca, NY 14853-2703, USA.
Sarah A Broadley
Thomas D Fox
Cornell University · US

Funding

TRANSLATIONAL CONTROL OF YEAST MITOCHONDRIAL GENESR01GM029362 · NIGMS · CORNELL UNIVERSITY ITHACA · PI FOX, THOMAS DAVID · 1985 to 2013
$6.1M
Nfs1p Function in Yeast MitochondriaF32GM065664 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI LUMPPIO, HEATHER L · 2002 to 2003
$68k
NIGMS NIH HHS F32 GM065664NIGMS NIH HHS GM29362NIGMS NIH HHS GM65664NIGMS NIH HHS R01 GM029362
6 · The paper itself

Abstract

The N-terminal and C-terminal domains of mitochondrially synthesized cytochrome c oxidase subunit II, Cox2, are translocated through the inner membrane to the intermembrane space (IMS). We investigated the distinct mechanisms of N-tail and C-tail export by analysis of epitope-tagged Cox2 variants encoded in Saccharomyces cerevisiae mitochondrial DNA. Both the N and C termini of a truncated protein lacking the Cox2 C-terminal domain were translocated to the IMS via a pathway dependent upon the conserved translocase Oxa1. The topology of this Cox2 variant, accumulated at steady state, was largely but not completely unaffected in mutants lacking proteins required for export of the C-tail domain, Cox18 and Mss2. C-tail export was blocked by truncation of the last 40 residues from the C-tail domain, indicating that sequence and/or structural features of this domain are required for its translocation. Mss2, a peripheral protein bound to the inner surface of the inner membrane, coimmunoprecipitated with full-length newly synthesized Cox2, whose leader peptide had already been cleaved in the IMS. Our data suggest that the C-tail domain is recognized posttranslationally by a specialized translocation apparatus after the N-tail has been translocated by Oxa1.

Indexed as

Electron Transport Complex IVImmunoprecipitationMembrane ProteinsMitochondriaMitochondrial MembranesMitochondrial ProteinsProtein BindingProtein Structure, TertiaryProtein TransportRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionThermodynamicsCOX18 protein, S cerevisiaecytochrome C oxidase subunit IIElectron Transport Complex IVMembrane ProteinsMitochondrial ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID17452441
PMCPMC1951498
OpenAlexW2120741711

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.