Evidence map›Paper›PMID 26904946›Full record

ArticleCell reports2016

Condensin Smc2-Smc4 Dimers Are Flexible and Dynamic.

Jorine M Eeftens, Allard J Katan, Marc Kschonsak, Markus Hassler, Liza de Wilde, Essam M Dief, Christian H Haering, Cees Dekker

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
7.1field-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

53 citing papers in PubMed, 97 citations in OpenAlex.

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  9. Motorized chain models of the ideal chromosome.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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  18. Genome folding through loop extrusion by SMC complexes.Nature reviews. Molecular cell biology · 2021
    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

8 authors at 2 institutions in 2 countries.

Jorine M EeftensDepartment of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, Delft 2628 CJ, the Netherlands.
Allard J KatanDepartment of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, Delft 2628 CJ, the Netherlands.
Marc KschonsakCell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), 69117 Heidelberg, Germany.
Markus HasslerCell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), 69117 Heidelberg, Germany.
Liza de WildeDepartment of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, Delft 2628 CJ, the Netherlands.
Essam M DiefDepartment of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, Delft 2628 CJ, the Netherlands.
Christian H HaeringCell Biology and Biophysics Unit, European Molecular Biology Laboratory (EMBL), 69117 Heidelberg, Germany. Electronic address: christian.haering@embl.de.
Cees DekkerDepartment of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, Delft 2628 CJ, the Netherlands. Electronic address: c.dekker@tudelft.nl.
Delft University of Technology · NLEuropean Molecular Biology Laboratory · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural maintenance of chromosomes (SMC) protein complexes, including cohesin and condensin, play key roles in the regulation of higher-order chromosome organization. Even though SMC proteins are thought to mechanistically determine the function of the complexes, their native conformations and dynamics have remained unclear. Here, we probe the topology of Smc2-Smc4 dimers of the S. cerevisiae condensin complex with high-speed atomic force microscopy (AFM) in liquid. We show that the Smc2-Smc4 coiled coils are highly flexible polymers with a persistence length of only ∼ 4 nm. Moreover, we demonstrate that the SMC dimers can adopt various architectures that interconvert dynamically over time, and we find that the SMC head domains engage not only with each other, but also with the hinge domain situated at the other end of the ∼ 45-nm-long coiled coil. Our findings reveal structural properties that provide insights into the molecular mechanics of condensin complexes.

Indexed as

Protein MultimerizationCarrier ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneChromosomes, FungalGene ExpressionImage Processing, Computer-AssistedMicroscopy, Atomic ForceMolecular Dynamics SimulationMolecular ImagingMonte Carlo MethodNuclear ProteinsProtein DomainsProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCarrier ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneNuclear ProteinsSaccharomyces cerevisiae ProteinsSMC2 protein, S cerevisiaeSMC4 protein, S cerevisiae

Identifiers

PMID26904946
PMCPMC4785793
OpenAlexW2275797864

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.