skip to main content
Language:
Search Limited to: Search Limited to: Resource type Show Results with: Show Results with: Search type Index

Formation of Chromatin Subcompartments by Phase Separation

Biophysical journal, 2018-05, Vol.114 (10), p.2262-2270 [Peer Reviewed Journal]

2018 Biophysical Society ;Copyright © 2018 Biophysical Society. Published by Elsevier Inc. All rights reserved. ;2018 Biophysical Society. 2018 Biophysical Society ;ISSN: 0006-3495 ;EISSN: 1542-0086 ;DOI: 10.1016/j.bpj.2018.03.011 ;PMID: 29628210

Full text available

Citations Cited by
  • Title:
    Formation of Chromatin Subcompartments by Phase Separation
  • Author: Erdel, Fabian ; Rippe, Karsten
  • Subjects: Biophysical s ; Chromatin - chemistry ; Chromatin - metabolism ; Models, Biological
  • Is Part Of: Biophysical journal, 2018-05, Vol.114 (10), p.2262-2270
  • Description: Chromatin is partitioned on multiple length scales into subcompartments that differ from each other with respect to their molecular composition and biological function. It is a key question how these compartments can form even though diffusion constantly mixes the nuclear interior and rapidly balances concentration gradients of soluble nuclear components. Different biophysical concepts are currently used to explain the formation of “chromatin bodies” in a self-organizing manner and without consuming energy. They rationalize how soluble protein factors that are dissolved in the liquid nuclear phase, the nucleoplasm, bind and organize transcriptionally active or silenced chromatin domains. In addition to cooperative binding of proteins to a preformed chromatin structure, two different mechanisms for the formation of phase-separated chromatin subcompartments have been proposed. One is based on bridging proteins that cross-link polymer segments with particular properties. Bridging can induce a collapse of the nucleosome chain and associated factors into an ordered globular phase. The other mechanism is based on multivalent interactions among soluble molecules that bind to chromatin. These interactions can induce liquid-liquid phase separation, which drives the assembly of liquid-like nuclear bodies around the respective binding sites on chromatin. Both phase separation mechanisms can explain that chromatin bodies are dynamic spherical structures, which can coalesce and are in constant and rapid exchange with the surrounding nucleoplasm. However, they make distinct predictions about how the size, density, and stability of chromatin bodies depends on the concentration and interaction behavior of the molecules involved. Here, we compare the different biophysical mechanisms for the assembly of chromatin bodies and discuss experimental strategies to distinguish them from each other. Furthermore, we outline the implications for the establishment and memory of functional chromatin state patterns.
  • Publisher: United States: Elsevier Inc
  • Language: English
  • Identifier: ISSN: 0006-3495
    EISSN: 1542-0086
    DOI: 10.1016/j.bpj.2018.03.011
    PMID: 29628210
  • Source: Open Access: PubMed Central
    MEDLINE
    Open Access: Cell Press Free Archives
Back to results list
Go to Previous pagePrevious Result  2 NextGo to Next page
INSPIRE LIBRARY - TON DUC THANG UNIVERSITY (84-028) 37 755 057 Feedback
19 Nguyen Huu Tho St. Dist.7, HCM thuvien@tdtu.edu.vn

Copyright © 2017 INSPIRE LIBRARY - TON DUC THANG UNIVERSITY

Searching Remote Databases, Please Wait