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Nucleic Acids Res. 2015 Oct 30;43(19):9097-106. doi: 10.1093/nar/gkv929. Epub 2015 Sep 24.

Methylation of histone H3 lysine 9 occurs during translation.

Author information

1
Fundación Ciencia & Vida, 7780272, Santiago, Chile.
2
Munich Center of Integrated Protein Science and Adolf-Butenandt Institute, 80336 Muenchen, Germany.
3
Institut Curie, Centre de Recherche, Paris, F-75248, France CNRS, UMR3664, Paris, F-75248, France Equipe Labellisee Ligue contre le Cancer, UMR3664, Paris, F-75248, France UPMC, UMR3664, Paris, F-75248, France Sorbonne University, PSL, France.
4
Fundación Ciencia & Vida, 7780272, Santiago, Chile aloyola@cienciavida.org.

Abstract

Histone post-translational modifications are key contributors to chromatin structure and function, and participate in the maintenance of genome stability. Understanding the establishment and maintenance of these marks, along with their misregulation in pathologies is thus a major focus in the field. While we have learned a great deal about the enzymes regulating histone modifications on nucleosomal histones, much less is known about the mechanisms establishing modifications on soluble newly synthesized histones. This includes methylation of lysine 9 on histone H3 (H3K9), a mark that primes the formation of heterochromatin, a critical chromatin landmark for genome stability. Here, we report that H3K9 mono- and dimethylation is imposed during translation by the methyltransferase SetDB1. We discuss the importance of these results in the context of heterochromatin establishment and maintenance and new therapeutic opportunities in pathologies where heterochromatin is perturbed.

PMID:
26405197
PMCID:
PMC4627087
DOI:
10.1093/nar/gkv929
[Indexed for MEDLINE]
Free PMC Article

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