Evidence map›Paper›PMID 41631486›Full record

ArticleNucleic acids research2026

Yeast condensin acts as a transient intermolecular crosslinker in entangled DNA.

Filippo Conforto, Antonio Valdes, Willem Vanderlinden, Davide Michieletto

Abstract read
In one paragraph

Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

Filippo ConfortoSchool of Physics and Astronomy, University of Edinburgh, Peter Guthrie Tait Road, Edinburgh EH9 3FD, United Kingdom.
Antonio ValdesChair of Biochemistry and Cell Biology, Theodor-Boveri-Institute, Julius Maximilian University of Würzburg, 97074 Würzburg, Germany.
Willem VanderlindenSchool of Physics and Astronomy, University of Edinburgh, Peter Guthrie Tait Road, Edinburgh EH9 3FD, United Kingdom.
Davide MichielettoSchool of Physics and Astronomy, University of Edinburgh, Peter Guthrie Tait Road, Edinburgh EH9 3FD, United Kingdom.ORCID 0000-0003-2186-6869

Funding

ERCEuropean Research Council 947918European Research Council CA17139Royal Society
6 · The paper itself

Abstract

Structural-Maintenance-of-Chromosome (SMC) complexes, such as condensins, organise the folding of chromosomes. However, their role in modulating the entanglement of DNA and chromatin is not fully understood. To address this question, we perform single-molecule and bulk characterisation of yeast condensin in entangled DNA. First, we discover that yeast condensin can proficiently bind double-stranded DNA through its hinge domain, in addition to its heads. Through bulk microrheology assays, we then discover that physiological concentrations of yeast condensin increase both the viscosity and elasticity of dense solutions of $\lambda$-DNA, suggesting that condensin acts as a crosslinker in entangled DNA, stabilising entanglements rather than resolving them and contrasting the popular theoretical picture where SMCs purely drive the formation of segregated, bottle-brush-like chromosome structures. We further discover that the presence of ATP fluidifies the solution-likely by activating loop extrusion-but does not recover the viscosity measured in the absence of protein. Finally, we show that the observed rheology can be understood by modelling SMCs as transient crosslinkers in bottle-brush-like entangled polymers. Our findings help us to understand how SMCs affect the dynamics and entanglement of genomes.

Indexed as

Adenosine TriphosphatasesDNADNA-Binding ProteinsMultiprotein ComplexesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphateDNA, FungalProtein BindingRheologyViscosityAdenosine TriphosphatasesAdenosine Triphosphatecondensin complexesDNADNA-Binding ProteinsDNA, FungalMultiprotein ComplexesSaccharomyces cerevisiae Proteins

Identifiers

PMID41631486
PMCPMC12865461

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.