Evidence map›Paper›PMID 24837193›Full record

ArticleNature structural & molecular biology2014

Association of condensin with chromosomes depends on DNA binding by its HEAT-repeat subunits.

Ilaria Piazza, Anna Rutkowska, Alessandro Ori, Marta Walczak, Jutta Metz, Vicent Pelechano, Martin Beck, Christian H Haering

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

68 citing papers in PubMed, 115 citations in OpenAlex.

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  16. Ycs4 Subunit ofBiochemistry · 2021
    Article
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  19. Genome folding through loop extrusion by SMC complexes.Nature reviews. Molecular cell biology · 2021
    Review
  20. Review

8 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 2 countries.

Ilaria Piazza1] Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany. [2] Structural and Computational Biology Unit, EMBL, Heidelberg, Germany. [3] International PhD Programme, EMBL, Heidelberg, Germany.
Anna Rutkowska1] Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany. [2] Structural and Computational Biology Unit, EMBL, Heidelberg, Germany.
Alessandro OriStructural and Computational Biology Unit, EMBL, Heidelberg, Germany.
Marta Walczak1] Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany. [2] Structural and Computational Biology Unit, EMBL, Heidelberg, Germany. [3].
Jutta Metz1] Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany. [2] Structural and Computational Biology Unit, EMBL, Heidelberg, Germany.
Vicent PelechanoGenome Biology Unit, EMBL, Heidelberg, Germany.
Martin BeckStructural and Computational Biology Unit, EMBL, Heidelberg, Germany.ORCID 0000000273971321
Christian H Haering1] Cell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany. [2] Structural and Computational Biology Unit, EMBL, Heidelberg, Germany.
European Molecular Biology Laboratory · DEEuropean Bioinformatics Institute · GBEuropean Molecular Biology Organization · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Condensin complexes have central roles in the three-dimensional organization of chromosomes during cell divisions, but how they interact with chromatin to promote chromosome segregation is largely unknown. Previous work has suggested that condensin, in addition to encircling chromatin fibers topologically within the ring-shaped structure formed by its SMC and kleisin subunits, contacts DNA directly. Here we describe the discovery of a binding domain for double-stranded DNA formed by the two HEAT-repeat subunits of the Saccharomyces cerevisiae condensin complex. From detailed mapping data of the interfaces between the HEAT-repeat and kleisin subunits, we generated condensin complexes that lack one of the HEAT-repeat subunits and consequently fail to associate with chromosomes in yeast and human cells. The finding that DNA binding by condensin's HEAT-repeat subunits stimulates the SMC ATPase activity suggests a multistep mechanism for the loading of condensin onto chromosomes.

Indexed as

Adenosine TriphosphatasesBinding SitesChromosomesDNADNA-Binding ProteinsModels, MolecularMolecular Sequence DataMultiprotein ComplexesProtein SubunitsSaccharomyces cerevisiaeSequence AlignmentSequence Analysis, ProteinAdenosine Triphosphatasescondensin complexesDNADNA-Binding ProteinsMultiprotein ComplexesProtein Subunits

Identifiers

PMID24837193
OpenAlexW2089736577

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.