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dc.contributor.author
Das, Rakesh
dc.contributor.author
Sakaue, Takahiro
dc.contributor.author
Shivashankar G.V.
dc.contributor.author
Prost, Jacques
dc.contributor.author
Hiraiwa, Tetsuya
dc.date.accessioned
2023-01-17T09:11:58Z
dc.date.available
2023-01-12T08:11:27Z
dc.date.available
2023-01-17T09:11:58Z
dc.date.issued
2022-12-06
dc.identifier.issn
2050-084X
dc.identifier.other
10.7554/eLife.79901
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/591860
dc.identifier.doi
10.3929/ethz-b-000591860
dc.description.abstract
Spatial organization of chromatin plays a critical role in genome regulation. Previously, various types of affinity mediators and enzymes have been attributed to regulate spatial organization of chromatin from a thermodynamics perspective. However, at the mechanistic level, enzymes act in their unique ways and perturb the chromatin. Here, we construct a polymer physics model following the mechanistic scheme of Topoisomerase-II, an enzyme resolving topological constraints of chromatin, and investigate how it affects interphase chromatin organization. Our computer simulations demonstrate Topoisomerase-II's ability to phase separate chromatin into eu- and heterochromatic regions with a characteristic wall-like organization of the euchromatic regions. We realized that the ability of the euchromatic regions to cross each other due to enzymatic activity of Topoisomerase-II induces this phase separation. This realization is based on the physical fact that partial absence of self-avoiding interaction can induce phase separation of a system into its self-avoiding and non-self-avoiding parts, which we reveal using a mean-field argument. Furthermore, motivated from recent experimental observations, we extend our model to a bidisperse setting and show that the characteristic features of the enzymatic activity-driven phase separation survive there. The existence of these robust characteristic features, even under the non-localized action of the enzyme, highlights the critical role of enzymatic activity in chromatin organization.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
eLife Sciences Publications
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
How enzymatic activity is involved in chromatin organization
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
eLife
ethz.journal.volume
11
en_US
ethz.pages.start
e79901
en_US
ethz.size
18 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Cambridge
ethz.publication.status
published
en_US
ethz.date.deposited
2023-01-12T08:11:27Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2023-01-17T09:11:59Z
ethz.rosetta.lastUpdated
2024-02-02T19:27:41Z
ethz.rosetta.versionExported
true
ethz.COinS
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