Evidence map›Paper›PMID 21068384›Full record

ArticleThe Journal of biological chemistry2011

Cox25 teams up with Mss51, Ssc1, and Cox14 to regulate mitochondrial cytochrome c oxidase subunit 1 expression and assembly in Saccharomyces cerevisiae.

Flavia Fontanesi, Paula Clemente, Antoni Barrientos

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

49 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Review
  3. Allotopic expression ofLife science alliance · 2023
    Article
  4. Article
  5. Article
  6. Mechanisms and regulation of protein synthesis in mitochondria.Nature reviews. Molecular cell biology · 2021
    Review
  7. Article
  8. Review
  9. Functions of CytochromeInternational journal of molecular sciences · 2020
    Review
  10. Article
  11. Article
  12. Emerging Roles in the Biogenesis of CytochromeFrontiers in cell and developmental biology · 2019
    Review
  13. Article
  14. Review
  15. Article
  16. Mitochondrial cytochrome c oxidase biogenesis: Recent developments.Seminars in cell & developmental biology · 2018
    Review
  17. Review
  18. Article
  19. Article
  20. The Cox1 C-terminal domain is a central regulator of cytochromeThe Journal of biological chemistry · 2017
    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

3 authors at 2 institutions in 2 countries.

Flavia FontanesiDepartments of Neurology, University of Miami Miller School of Medicine, Miami, Florida 33136, USA.
Paula Clemente
Antoni Barrientos
Instituto de Investigaciones Biomédicas Sols-Morreale · ESUniversity of Miami · US

Funding

CYTOCHROME C OXIDASE IN HEALTH AND DISEASER01GM071775 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI BARRIENTOS, ANTONI · 2006 to 2015
$3.1M
NIGMS NIH HHS GM071775ANIGMS NIH HHS R01 GM071775
6 · The paper itself

Abstract

In the yeast Saccharomyces cerevisiae, mitochondrial cytochrome c oxidase (COX) biogenesis is translationally regulated. Mss51, a specific COX1 mRNA translational activator and Cox1 chaperone, drives the regulatory mechanism. During translation and post-translationally, newly synthesized Cox1 physically interacts with a complex of proteins involving Ssc1, Mss51, and Cox14, which eventually hand over Cox1 to the assembly pathway. This step is probably catalyzed by assembly chaperones such as Shy1 in a process coupled to the release of Ssc1-Mss51 from the complex. Impaired COX assembly results in the trapping of Mss51 in the complex, thus limiting its availability for COX1 mRNA translation. An exception is a null mutation in COX14 that does not affect Cox1 synthesis because the Mss51 trapping complexes become unstable, and Mss51 is readily available for translation. Here we present evidence showing that Cox25 is a new essential COX assembly factor that plays some roles similar to Cox14. A null mutation in COX25 by itself or in combination with other COX mutations does not affect Cox1 synthesis. Cox25 is an inner mitochondrial membrane intrinsic protein with a hydrophilic C terminus protruding into the matrix. Cox25 is an essential component of the complexes containing newly synthesized Cox1, Ssc1, Mss51, and Cox14. In addition, Cox25 is also found to interact with Shy1 and Cox5 in a complex that does not contain Mss51. These results suggest that once Ssc1-Mss51 are released from the Cox1 stabilization complex, Cox25 continues to interact with Cox14 and Cox1 to facilitate the formation of multisubunit COX assembly intermediates.

Indexed as

Gene Expression Regulation, FungalAmino Acid SequenceCalcium-Transporting ATPasesElectron Transport Complex IVGene DeletionMembrane ProteinsMitochondriaMitochondrial MembranesMitochondrial ProteinsMolecular ChaperonesMolecular Sequence DataSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSucroseTranscription FactorsCalcium-Transporting ATPasesCoa3 protein, S cerevisiaeCOX14 protein, S cerevisiaeCox1 protein, S cerevisiaeElectron Transport Complex IVMembrane ProteinsMitochondrial ProteinsMolecular ChaperonesMss51 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSHY1 protein, S cerevisiaeSSC1 protein, S cerevisiaeSucroseTranscription Factors

Identifiers

PMID21068384
PMCPMC3013015
OpenAlexW2087514312

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.