Dissecting the role of H3K64me3 in mouse pericentromeric heterochromatin

Ulrike C. Lange, Stéphanie Siebert, Mark Wossidlo, Thomas Weiss, Céline Ziegler-Birling, Jörn Walter, Maria-Elena Torres-Padilla, Sylvain Daujat () and Robert Schneider
Additional contact information
Ulrike C. Lange: Max-Planck-Institute of Immunobiology and Epigenetics
Stéphanie Siebert: Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS/INSERM/ULP
Mark Wossidlo: Saarland University
Thomas Weiss: Max-Planck-Institute of Immunobiology and Epigenetics
Céline Ziegler-Birling: Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS/INSERM/ULP
Jörn Walter: Saarland University
Maria-Elena Torres-Padilla: Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS/INSERM/ULP
Sylvain Daujat: Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS/INSERM/ULP
Robert Schneider: Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS/INSERM/ULP

Nature Communications, 2013, vol. 4, issue 1, 1-10

Abstract: Abstract To ensure genome stability, pericentromeric regions are compacted in a dense heterochromatic structure through a combination of specific ‘epigenetic’ factors and modifications. A cascadal pathway is responsible for establishing pericentromeric chromatin involving chromatin modifiers and ‘readers’, such as H3K9 histone methyltransferases (Suv)39h and heterochromatin protein 1. Here we define how H3K64me3 on the lateral surface of the histone octamer integrates within the heterochromatinization cascade. Our data suggest that enrichment of H3K64me3 at pericentromeric chromatin foci is dependent on H3K9me3 but independent of a number of central factors such as heterochromatin protein 1, DNA methyltransferases and Suv4-20h histone methyltransferases. Our results support a model in which pericentromeric heterochromatin foci are formed along distinct pathways upon H3K9 trimethylation, involving H3K64me3 to potentially stabilize DNA–histone interactions, as well as sequential recruitment of repressive histone tail and DNA modifications. We hence suggest that multiple mechanisms ensure heterochromatin integrity at pericentromeres, with H3K64me3 as an important factor.

Date: 2013
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms3233 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3233

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms3233

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().