Evidence map›Paper›PMID 24945319›Full record

ArticlePLoS genetics2014

CPF-associated phosphatase activity opposes condensin-mediated chromosome condensation.

Vincent Vanoosthuyse, Pénélope Legros, Sjaak J A van der Sar, Gaël Yvert, Kenji Toda, Thierry Le Bihan, Yoshinori Watanabe, Kevin Hardwick, Pascal Bernard

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

43 citing papers in PubMed, 60 citations in OpenAlex.

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  13. Dephosphorylation in nuclear reassembly after mitosis.Frontiers in cell and developmental biology · 2022
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  16. CDK9 keeps RNA polymerase II on track.Cellular and molecular life sciences : CMLS · 2021
    Review
  17. Article
  18. Review
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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

9 authors at 5 institutions in 3 countries.

Vincent VanoosthuyseCNRS, UMR5239, LBMC; Ecole Normale Supérieure de Lyon; Université Lyon 01, Lyon, France; Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, United Kingdom.
Pénélope LegrosCNRS, UMR5239, LBMC; Ecole Normale Supérieure de Lyon; Université Lyon 01, Lyon, France.
Sjaak J A van der SarWellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, United Kingdom.
Gaël YvertCNRS, UMR5239, LBMC; Ecole Normale Supérieure de Lyon; Université Lyon 01, Lyon, France.
Kenji TodaChromosome Dynamics, Institute of Molecular and Cellular Biosciences, The University of Tokyo, Yayoi, Bunkyo-ku, Tokyo, Japan.
Thierry Le BihanSynthSys Edinburgh, The University of Edinburgh, Edinburgh, United Kingdom.
Yoshinori WatanabeChromosome Dynamics, Institute of Molecular and Cellular Biosciences, The University of Tokyo, Yayoi, Bunkyo-ku, Tokyo, Japan.
Kevin HardwickWellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, United Kingdom.
Pascal BernardCNRS, UMR5239, LBMC; Ecole Normale Supérieure de Lyon; Université Lyon 01, Lyon, France.
Wellcome Centre for Cell Biology · GBCentre National de la Recherche Scientifique · FRThe University of Tokyo · JPUniversité Claude Bernard Lyon 1 · FRUniversity of Edinburgh · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D019621/1Wellcome Trust 077707Wellcome Trust 092076
6 · The paper itself

Abstract

Functional links connecting gene transcription and condensin-mediated chromosome condensation have been established in species ranging from prokaryotes to vertebrates. However, the exact nature of these links remains misunderstood. Here we show in fission yeast that the 3' end RNA processing factor Swd2.2, a component of the Cleavage and Polyadenylation Factor (CPF), is a negative regulator of condensin-mediated chromosome condensation. Lack of Swd2.2 does not affect the assembly of the CPF but reduces its association with chromatin. This causes only limited, context-dependent effects on gene expression and transcription termination. However, CPF-associated Swd2.2 is required for the association of Protein Phosphatase 1 PP1(Dis2) with chromatin, through an interaction with Ppn1, a protein that we identify as the fission yeast homologue of vertebrate PNUTS. We demonstrate that Swd2.2, Ppn1 and PP1Dis2 form an independent module within the CPF, which provides an essential function in the absence of the CPF-associated Ssu72 phosphatase. We show that Ppn1 and Ssu72, like Swd2.2, are also negative regulators of condensin-mediated chromosome condensation. We conclude that Swd2.2 opposes condensin-mediated chromosome condensation by facilitating the function of the two CPF-associated phosphatases PP1 and Ssu72.

Indexed as

AcetylationAcid Anhydride HydrolasesAdenosine TriphosphatasesCell Cycle ProteinsChromatinDNA-Binding ProteinsDNA Polymerase IIIHistone-Lysine N-MethyltransferaseHistonesmRNA Cleavage and Polyadenylation FactorsMultiprotein ComplexesPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 1Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAcid Anhydride HydrolasesAdenosine TriphosphatasesCell Cycle ProteinsChromatincondensin complexesDNA-Binding ProteinsDNA Polymerase IIIHistone-Lysine N-MethyltransferaseHistonesmRNA Cleavage and Polyadenylation FactorsMultiprotein ComplexesPhosphoprotein PhosphatasesPpn1 protein, S cerevisiaeProtein Phosphatase 1Saccharomyces cerevisiae ProteinsSSU72 protein, S cerevisiaeSWD2 protein, S cerevisiae

Identifiers

PMID24945319
PMCPMC4063703
OpenAlexW2081180101

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.