Evidence map›Paper›PMID 34329301›Full record

ArticlePLoS computational biology2021

Modeling of DNA binding to the condensin hinge domain using molecular dynamics simulations guided by atomic force microscopy.

Hiroki Koide, Noriyuki Kodera, Shveta Bisht, Shoji Takada, Tsuyoshi Terakawa

Abstract read
In one paragraph

Article in PLoS computational biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

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  7. Nucleic Acids and Electrical Signals.Reviews of physiology, biochemistry and pharmacology · 2025
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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

5 authors.

Hiroki KoideDepartment of Biophysics, Graduate School of Science, Kyoto University, Kyoto, Japan.ORCID 0000-0002-7468-6047
Noriyuki KoderaNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.ORCID 0000-0003-4880-8423
Shveta BishtCell Biology and Biophysics Unit, Structural and Computational Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID 0000-0002-5566-3472
Shoji TakadaDepartment of Biophysics, Graduate School of Science, Kyoto University, Kyoto, Japan.ORCID 0000-0001-5385-7217
Tsuyoshi TerakawaDepartment of Biophysics, Graduate School of Science, Kyoto University, Kyoto, Japan.ORCID 0000-0002-0151-1123

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The condensin protein complex compacts chromatin during mitosis using its DNA-loop extrusion activity. Previous studies proposed scrunching and loop-capture models as molecular mechanisms for the loop extrusion process, both of which assume the binding of double-strand (ds) DNA to the hinge domain formed at the interface of the condensin subunits Smc2 and Smc4. However, how the hinge domain contacts dsDNA has remained unknown. Here, we conducted atomic force microscopy imaging of the budding yeast condensin holo-complex and used this data as basis for coarse-grained molecular dynamics simulations to model the hinge structure in a transient open conformation. We then simulated the dsDNA binding to open and closed hinge conformations, predicting that dsDNA binds to the outside surface when closed and to the outside and inside surfaces when open. Our simulations also suggested that the hinge can close around dsDNA bound to the inside surface. Based on these simulation results, we speculate that the conformational change of the hinge domain might be essential for the dsDNA binding regulation and play roles in condensin-mediated DNA-loop extrusion.

Indexed as

Adenosine TriphosphatasesBinding SitesComputational BiologyComputer SimulationDNA-Binding ProteinsDNA, FungalMicroscopy, Atomic ForceModels, BiologicalModels, MolecularMolecular Dynamics SimulationMultiprotein ComplexesProtein ConformationProtein Interaction Domains and MotifsSaccharomyces cerevisiae ProteinsStatic ElectricityAdenosine Triphosphatasescondensin complexesDNA-Binding ProteinsDNA, FungalMultiprotein ComplexesSaccharomyces cerevisiae Proteins

Identifiers

PMID34329301
PMCPMC8357123

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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.