Evidence map›Paper›PMID 16624818›Full record

ArticleThe Journal of biological chemistry2006

Complementation of Saccharomyces cerevisiae coq7 mutants by mitochondrial targeting of the Escherichia coli UbiF polypeptide: two functions of yeast Coq7 polypeptide in coenzyme Q biosynthesis.

UyenPhuong C Tran, Beth Marbois, Peter Gin, Melissa Gulmezian, Tanya Jonassen, Catherine F Clarke

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
1.1field-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

39 citing papers in PubMed, 63 citations in OpenAlex.

  1. Understanding coenzyme Q.Physiological reviews · 2024
    Review
  2. Article
  3. Article
  4. Article
  5. Manganese-driven CoQ deficiency.Nature communications · 2022
    Article
  6. Article
  7. Article
  8. Cellular Models for Primary CoQ Deficiency Pathogenesis Study.International journal of molecular sciences · 2021
    Review
  9. Article
  10. Article
  11. The Journal of biological chemistry · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Coenzyme QEssays in biochemistry · 2018
    Review
  17. Review
  18. Biochemistry of Mitochondrial Coenzyme Q Biosynthesis.Trends in biochemical sciences · 2017
    Review
  19. Human COQ9 Rescues aFrontiers in physiology · 2017
    Article
  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

6 authors at 1 institution in 1 country.

UyenPhuong C TranDepartment of Chemistry and Biochemistry, and Molecular Biology Institute, University of California-Los Angeles, 607 Charles E. Young Drive East, Los Angeles, CA 90095, USA.
Beth Marbois
Peter Gin
Melissa Gulmezian
Tanya Jonassen
Catherine F Clarke
University of California, Los Angeles · US

Funding

FUNCTIONAL ROLES OF UBIQUINONE IN YEAST AND HUMAN CELLSR01GM045952 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CLARKE, CATHERINE FREITAG · 1991 to 2009
$3.2M
NIGMS NIH HHS GM 45952NIGMS NIH HHS R01 GM045952
6 · The paper itself

Abstract

Coenzyme Q (ubiquinone or Q) functions in the respiratory electron transport chain and serves as a lipophilic antioxidant. In the budding yeast Saccharomyces cerevisiae, Q biosynthesis requires nine Coq proteins (Coq1-Coq9). Previous work suggests both an enzymatic activity and a structural role for the yeast Coq7 protein. To define the functional roles of yeast Coq7p we test whether Escherichia coli ubiF can functionally substitute for yeast COQ7. The ubiF gene encodes a flavin-dependent monooxygenase that shares no homology to the Coq7 protein and is required for the final monooxygenase step of Q biosynthesis in E. coli. The ubiF gene expressed at low copy restores growth of a coq7 point mutant (E194K) on medium containing a non-fermentable carbon source, but fails to rescue a coq7 null mutant. However, expression of ubiF from a multicopy vector restores growth and Q synthesis for both mutants, although with a higher efficiency in the point mutant. We attribute the more efficient rescue of the coq7 point mutant to higher steady state levels of the Coq3, Coq4, and Coq6 proteins and to the presence of demethoxyubiquinone, the substrate of UbiF. Coq7p co-migrates with the Coq3 and Coq4 polypeptides as a high molecular mass complex. Here we show that addition of Q to the growth media also stabilizes the Coq3 and Coq4 polypeptides in the coq7 null mutant. The data suggest that Coq7p, and the lipid quinones (demethoxyubiquinone and Q) function to stabilize other Coq polypeptides.

Indexed as

MutationAmino Acid SequenceElectrochemistryEscherichia coli ProteinsGenetic Complementation TestGenetic VectorsLipidsMitochondriaMixed Function OxygenasesModels, ChemicalMolecular Sequence DataPoint MutationSaccharomyces cerevisiaeSequence Homology, Amino AcidUbiquinoneEscherichia coli ProteinsLipidsMixed Function OxygenasesUbiF protein, E coliUbiquinone

Identifiers

PMID16624818
PMCPMC3066048
OpenAlexW1963917155

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.