Evidence map›Paper›PMID 22095077›Full record

ArticleGenetics2012

Multiple roles of the Cox20 chaperone in assembly of Saccharomyces cerevisiae cytochrome c oxidase.

Leah E Elliott, Scott A Saracco, Thomas D Fox

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

26 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. A Role forMicroorganisms · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Mitochondrial cytochrome c oxidase biogenesis: Recent developments.Seminars in cell & developmental biology · 2018
    Review
  18. Building the CuThe Journal of biological chemistry · 2018
    Review
  19. The mitochondrial TMEM177 associates with COX20 during COX2 biogenesis.Biochimica et biophysica acta. Molecular cell research · 2018
    Article
  20. Multifunctional Mitochondrial AAA Proteases.Frontiers in molecular biosciences · 2017
    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.

Leah E ElliottDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853-2703, USA.
Scott A Saracco
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
PREDOCTORAL TRAINING IN GENETICS AND DEVELOPMENTT32GM007617 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BARBASH, DANIEL A · 1985 to 2021
$5.5M
NIGMS NIH HHS R01 GM029362NIGMS NIH HHS R01GM29362NIGMS NIH HHS T32 GM007617NIGMS NIH HHS T32GM007617
6 · The paper itself

Abstract

The Cox2 subunit of Saccharomyces cerevisiae cytochrome c oxidase is synthesized in the mitochondrial matrix as a precursor whose leader peptide is rapidly processed by the inner membrane protease following translocation to the intermembrane space. Processing is chaperoned by Cox20, an integral inner membrane protein whose hydrophilic domains are located in the intermembrane space, and Cox20 remains associated with mature, unassembled Cox2. The Cox2 C-tail domain is exported post-translationally by the highly conserved translocase Cox18 and associated proteins. We have found that Cox20 is required for efficient export of the Cox2 C-tail. Furthermore, Cox20 interacts by co-immune precipitation with Cox18, and this interaction requires the presence of Cox2. We therefore propose that Cox20 binding to Cox2 on the trans side of the inner membrane accelerates dissociation of newly exported Cox2 from the Cox18 translocase, promoting efficient cycling of the translocase. The requirement for Cox20 in cytochrome c oxidase assembly and respiratory growth is partially bypassed by yme1, mgr1 or mgr3 mutations, each of which reduce i-AAA protease activity in the intermembrane space. Thus, Cox20 also appears to stabilize unassembled Cox2 against degradation by the i-AAA protease. Pre-Cox2 leader peptide processing by Imp1 occurs in the absence of Cox20 and i-AAA protease activity, but is greatly reduced in efficiency. Under these conditions some mature Cox2 is assembled into cytochrome c oxidase allowing weak respiratory growth. Thus, the Cox20 chaperone has important roles in leader peptide processing, C-tail export, and stabilization of Cox2.

Indexed as

Electron Transport Complex IVEndopeptidasesMembrane ProteinsMitochondrial ProteinsMolecular ChaperonesMutationProtein BindingProtein Sorting SignalsProtein StabilityProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCOX18 protein, S cerevisiaeCox20 protein, S cerevisiaeElectron Transport Complex IVEndopeptidasesIMP1 protein, S cerevisiaeMembrane ProteinsMitochondrial ProteinsMolecular ChaperonesProtein Sorting SignalsSaccharomyces cerevisiae Proteins

Identifiers

PMID22095077
PMCPMC3276622
OpenAlexW2139282193

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.