Evidence map›Paper›PMID 29949571›Full record

ArticlePLoS biology2018

Condensin ATPase motifs contribute differentially to the maintenance of chromosome morphology and genome stability.

Roger Palou, Thillaivillalan Dhanaraman, Rim Marrakchi, Mirela Pascariu, Mike Tyers, Damien D'Amours

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

17 citing papers in PubMed, 22 citations in OpenAlex.

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  8. Cohesin organization, dynamics, and subdomain functions revealed by genetic suppressor screening.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023
    Article
  9. Cohesin ATPase activities regulate DNA binding and coiled-coil configuration.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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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

6 authors at 2 institutions in 1 country.

Roger PalouInstitute for Research in Immunology and Cancer, Département de Pathologie et Biologie Cellulaire, Université de Montréal, Montréal, Québec, Canada.
Thillaivillalan DhanaramanInstitute for Research in Immunology and Cancer, Département de Pathologie et Biologie Cellulaire, Université de Montréal, Montréal, Québec, Canada.
Rim MarrakchiInstitute for Research in Immunology and Cancer, Département de Pathologie et Biologie Cellulaire, Université de Montréal, Montréal, Québec, Canada.
Mirela PascariuInstitute for Research in Immunology and Cancer, Département de Pathologie et Biologie Cellulaire, Université de Montréal, Montréal, Québec, Canada.
Mike TyersInstitute for Research in Immunology and Cancer, Département de Pathologie et Biologie Cellulaire, Université de Montréal, Montréal, Québec, Canada.
Damien D'AmoursInstitute for Research in Immunology and Cancer, Département de Pathologie et Biologie Cellulaire, Université de Montréal, Montréal, Québec, Canada.ORCID 0000-0002-2183-9951
Institute for Research in Immunology and Cancer · CAUniversity of Ottawa · CA

Funding

Canadian Institutes of Health Research MOP 136788Canadian Institutes of Health Research MOP 366608Canadian Institutes of Health Research MOP 82912Canadian Institutes of Health Research PJT 148969
6 · The paper itself

Abstract

Effective transfer of genetic information during cell division requires a major reorganization of chromosome structure. This process is triggered by condensin, a conserved pentameric ATPase essential for chromosome condensation. How condensin harnesses the energy of ATP hydrolysis to promote chromatin reorganization is unknown. To address this issue, we performed a genetic screen specifically focused on the ATPase domain of Smc4, a core subunit of condensin. Our screen identified mutational hotspots that impair condensin's ability to condense chromosomes to various degrees. These mutations have distinct effects on viability, genome stability, and chromosome morphology, revealing unique thresholds for condensin enzymatic activity in the execution of its cellular functions. Biochemical analyses indicate that inactivation of Smc4 ATPase activity can result in cell lethality because it favors a specific configuration of condensin that locks ATP in the enzyme. Together, our results provide critical insights into the mechanism used by condensin to harness the energy of ATP hydrolysis for the compaction of chromatin.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateChromatinChromosomal Proteins, Non-HistoneChromosomesDNA-Binding ProteinsGenomic InstabilityMitosisMultiprotein ComplexesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesAdenosine TriphosphateChromatinChromosomal Proteins, Non-Histonecondensin complexesDNA-Binding ProteinsMultiprotein ComplexesSaccharomyces cerevisiae ProteinsSMC4 protein, S cerevisiae

Identifiers

PMID29949571
PMCPMC6039025
OpenAlexW2810059769

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.