Evidence map›Paper›PMID 23091701›Full record

ArticleOpen biology2012

Impaired coenzyme A synthesis in fission yeast causes defective mitosis, quiescence-exit failure, histone hypoacetylation and fragile DNA.

Takahiro Nakamura, Tomáš Pluskal, Yukinobu Nakaseko, Mitsuhiro Yanagida

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Is There a Histone Code for Cellular Quiescence?Frontiers in cell and developmental biology · 2021
    Review
  5. Article
  6. Article
  7. Review
  8. Article
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  11. Simultaneous and absolute quantification of nucleoside triphosphates using liquid chromatography-triple quadrupole tandem mass spectrometry.Genes and environment : the official journal of the Japanese Environmental Mutagen Society · 2018
    Article
  12. Review
  13. Article
  14. Article
  15. Article
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  17. Article
  18. 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

4 authors at 2 institutions in 1 country.

Takahiro NakamuraOkinawa Institute of Science and Technology Graduate University, Tancha 1919-1, Onna, Okinawa 904-0495, Japan.
Tomáš Pluskal
Yukinobu Nakaseko
Mitsuhiro Yanagida
Okinawa Institute of Science and Technology Graduate University · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biosynthesis of coenzyme A (CoA) requires a five-step process using pantothenate and cysteine in the fission yeast Schizosaccharomyces pombe. CoA contains a thiol (SH) group, which reacts with carboxylic acid to form thioesters, giving rise to acyl-activated CoAs such as acetyl-CoA. Acetyl-CoA is essential for energy metabolism and protein acetylation, and, in higher eukaryotes, for the production of neurotransmitters. We isolated a novel S. pombe temperature-sensitive strain ppc1-537 mutated in the catalytic region of phosphopantothenoylcysteine synthetase (designated Ppc1), which is essential for CoA synthesis. The mutant becomes auxotrophic to pantothenate at permissive temperature, displaying greatly decreased levels of CoA, acetyl-CoA and histone acetylation. Moreover, ppc1-537 mutant cells failed to restore proliferation from quiescence. Ppc1 is thus the product of a super-housekeeping gene. The ppc1-537 mutant showed combined synthetic lethal defects with five of six histone deacetylase mutants, whereas sir2 deletion exceptionally rescued the ppc1-537 phenotype. In synchronous cultures, ppc1-537 cells can proceed to the S phase, but lose viability during mitosis failing in sister centromere/kinetochore segregation and nuclear division. Additionally, double-strand break repair is defective in the ppc1-537 mutant, producing fragile broken DNA, probably owing to diminished histone acetylation. The CoA-supported metabolism thus controls the state of chromosome DNA.

Indexed as

AcetylationAmino Acid SequenceCell Cycle CheckpointsCoenzyme ADNA Breaks, Double-StrandedDNA, FungalDNA RepairGenes, FungalHistone AcetyltransferasesHistone DeacetylasesHistonesMitosisMolecular Sequence DataMutationPeptide SynthasesRadiation ToleranceCoenzyme ADNA, FungalHistone AcetyltransferasesHistone DeacetylasesHistonesPeptide Synthasesphosphopantothenoyl-cysteine synthetaseSchizosaccharomyces pombe Proteinsacetyl-CoAcentromere/kinetochorelipid dropletpantothenatephosphopantothenoylcysteine synthetase

Identifiers

PMID23091701
PMCPMC3472395
OpenAlexW2008649238

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.