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

Liquid-Liquid Phase Separation of Histone Proteins in Cells: Role in Chromatin Organization

Biophysical journal, 2020-02, Vol.118 (3), p.753-764 [Peer Reviewed Journal]

2019 Biophysical Society ;Copyright © 2019 Biophysical Society. Published by Elsevier Inc. All rights reserved. ;2019 Biophysical Society. 2019 Biophysical Society ;ISSN: 0006-3495 ;EISSN: 1542-0086 ;DOI: 10.1016/j.bpj.2019.12.022 ;PMID: 31952807

Full text available

Citations Cited by
  • Title:
    Liquid-Liquid Phase Separation of Histone Proteins in Cells: Role in Chromatin Organization
  • Author: Shakya, Anisha ; Park, Seonyoung ; Rana, Neha ; King, John T.
  • Subjects: Chromatin ; Chromobox Protein Homolog 5 ; HeLa Cells ; Heterochromatin ; Histones - genetics ; Humans ; Nucleosomes
  • Is Part Of: Biophysical journal, 2020-02, Vol.118 (3), p.753-764
  • Description: Liquid-liquid phase separation (LLPS) of proteins and nucleic acids has emerged as an important phenomenon in membraneless intracellular organization. We demonstrate that the linker histone H1 condenses into liquid-like droplets in the nuclei of HeLa cells. The droplets, observed during the interphase of the cell cycle, are colocalized with DNA-dense regions indicative of heterochromatin. In vitro, H1 readily undergoes LLPS with both DNA and nucleosomes of varying lengths but does not phase separate in the absence of DNA. The nucleosome core particle maintains its structural integrity inside the droplets, as demonstrated by FRET. Unexpectedly, H2A also forms droplets in the presence of DNA and nucleosomes in vitro, whereas the other core histones precipitate. The phase diagram of H1 with nucleosomes is invariant to the nucleosome length at physiological salt concentration, indicating that H1 is capable of partitioning large segments of DNA into liquid-like droplets. Of the proteins tested (H1, core histones, and the heterochromatin protein HP1α), this property is unique to H1. In addition, free nucleotides promote droplet formation of H1 nucleosome in a nucleotide-dependent manner, with droplet formation being most favorable with ATP. Although LLPS of HP1α is known to contribute to the organization of heterochromatin, our results indicate that H1 also plays a role. Based on our study, we propose that H1 and DNA act as scaffolds for phase-separated heterochromatin domains.
  • Publisher: United States: Elsevier Inc
  • Language: English
  • Identifier: ISSN: 0006-3495
    EISSN: 1542-0086
    DOI: 10.1016/j.bpj.2019.12.022
    PMID: 31952807
  • Source: Cell Press Free Archives
    MEDLINE
    PubMed Central
Back to results list
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