English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Dynamic and flexible H3K9me3 bridging via HP1beta dimerization establishes a plastic state of condensed chromatin.

Hiragami-Hamada, K., Sörös, S., Nikolov, M., Wilkins, B., Kreuz, S., Chen, C., et al. (2016). Dynamic and flexible H3K9me3 bridging via HP1beta dimerization establishes a plastic state of condensed chromatin. Nature Communications, 7: 11310 (2016). doi:10.1038/ncomms11310.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files
hide Files
:
Hiragami et al..pdf (Publisher version), 5MB
 
File Permalink:
-
Name:
Hiragami et al..pdf
Description:
-
Visibility:
Restricted (Max Planck Institute of Immunobiology and Epigenetics, MFIB; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Locator:
https://www.nature.com/articles/ncomms11310 (Publisher version)
Description:
-

Creators

show
hide
 Creators:
Hiragami-Hamada, K.1, Author              
Sörös, S.1, Author              
Nikolov, M.1, Author              
Wilkins, B.1, Author
Kreuz, S.1, Author              
Chen, C.1, Author
De La Rosa-Velazquez, I. A.2, Author
Zenn, H. M.1, Author
Kost, N.1, Author              
Pohl, W.1, Author              
Chernev, A.1, Author
Schwarzer, D.1, Author
Jenuwein, Thomas2, Author              
Lorincz, M.1, Author
Zimmermann, B.1, Author
Walla, P. J.1, Author              
Neumann, H.1, Author
Baubec, T.1, Author
Urlaub, H.1, Author              
Fischle, W.1, Author              
Affiliations:
1External Organizations, ou_persistent22              
2Department of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243644              

Content

show
hide
Free keywords: -
 Abstract: Histone H3 trimethylation of lysine 9 (H3K9me3) and proteins of the heterochromatin protein 1 (HP1) family are hallmarks of heterochromatin, a state of compacted DNA essential for genome stability and long-term transcriptional silencing. The mechanisms by which H3K9me3 and HP1 contribute to chromatin condensation have been speculative and controversial. Here we demonstrate that human HP1beta is a prototypic HP1 protein exemplifying most basal chromatin binding and effects. These are caused by dimeric and dynamic interaction with highly enriched H3K9me3 and are modulated by various electrostatic interfaces. HP1beta bridges condensed chromatin, which we postulate stabilizes the compacted state. In agreement, HP1beta genome-wide localization follows H3K9me3-enrichment and artificial bridging of chromatin fibres is sufficient for maintaining cellular heterochromatic conformation. Overall, our findings define a fundamental mechanism for chromatin higher order structural changes caused by HP1 proteins, which might contribute to the plastic nature of condensed chromatin.

Details

show
hide
Language(s): eng - English
 Dates: 2016-04-19
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/ncomms11310
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Nature Publishing Group
Pages: 16 Volume / Issue: 7 Sequence Number: 11310 (2016) Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723