Evidence map›Paper›PMID 32479562›Full record

ArticlePloS one2020

Intragenic suppressor mutations of the COQ8 protein kinase homolog restore coenzyme Q biosynthesis and function in Saccharomyces cerevisiae.

Agape M Awad, Anish Nag, Nguyen V B Pham, Michelle C Bradley, Nour Jabassini, Juan Nathaniel, Catherine F Clarke

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. No Chance to Survive:Antibiotics (Basel, Switzerland) · 2023
    Article
  3. 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

7 authors at 1 institution in 1 country.

Agape M AwadDepartment of Chemistry and Biochemistry, and the Molecular Biology Institute, University of California, Los Angeles, California, United States of America.
Anish NagDepartment of Chemistry and Biochemistry, and the Molecular Biology Institute, University of California, Los Angeles, California, United States of America.
Nguyen V B PhamDepartment of Chemistry and Biochemistry, and the Molecular Biology Institute, University of California, Los Angeles, California, United States of America.
Michelle C BradleyDepartment of Chemistry and Biochemistry, and the Molecular Biology Institute, University of California, Los Angeles, California, United States of America.
Nour JabassiniDepartment of Chemistry and Biochemistry, and the Molecular Biology Institute, University of California, Los Angeles, California, United States of America.
Juan NathanielDepartment of Chemistry and Biochemistry, and the Molecular Biology Institute, University of California, Los Angeles, California, United States of America.
Catherine F ClarkeDepartment of Chemistry and Biochemistry, and the Molecular Biology Institute, University of California, Los Angeles, California, United States of America.ORCID 0000-0002-6426-3833
University of California, Los Angeles · US

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
NIGMS NIH HHS T32 GM007185
6 · The paper itself

Abstract

Saccharomyces cerevisiae Coq8 is a member of the ancient UbiB atypical protein kinase family. Coq8, and its orthologs UbiB, ABC1, ADCK3, and ADCK4, are required for the biosynthesis of coenzyme Q in yeast, E. coli, A. thaliana, and humans. Each Coq8 ortholog retains nine highly conserved protein kinase-like motifs, yet its functional role in coenzyme Q biosynthesis remains mysterious. Coq8 may function as an ATPase whose activity is stimulated by coenzyme Q intermediates and phospholipids. A key yeast point mutant expressing Coq8-A197V was previously shown to result in a coenzyme Q-less, respiratory deficient phenotype. The A197V substitution occurs in the crucial Ala-rich protein kinase-like motif I of yeast Coq8. Here we show that long-term cultures of mutants expressing Coq8-A197V produce spontaneous revertants with the ability to grow on medium containing a non-fermentable carbon source. Each revertant is shown to harbor a secondary intragenic suppressor mutation within the COQ8 gene. The intragenic suppressors restore the synthesis of coenzyme Q. One class of the suppressors fully restores the levels of coenzyme Q and key Coq polypeptides necessary for the maintenance and integrity of the high-molecular mass CoQ synthome (also termed complex Q), while the other class provides only a partial rescue. Mutants harboring the first class of suppressors grow robustly under respiratory conditions, while mutants containing the second class grow more slowly under these conditions. Our work provides insight into the function of this important yet still enigmatic Coq8 family.

Indexed as

Suppression, GeneticAmino Acid SubstitutionAsparagineCulture MediaGene Expression Regulation, FungalProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquinoneAsparagineCOQ8 protein, S cerevisiaeCulture MediaSaccharomyces cerevisiae ProteinsUbiquinone

Identifiers

PMID32479562
PMCPMC7263595
OpenAlexW3029142014

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.