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Methylation of histone H3 lysine 9 occurs during translation
Author(s) -
Carlos Rondón,
Francisco Saavedra,
Francisca Alvarez,
César Díaz-Celis,
Valentina Ugalde,
Jianhua Li,
Ignasi Forné,
Zachary A. GurardLevin,
Geneviève Almouzni,
Axel Imhof,
Alejandra Loyola
Publication year - 2015
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/gkv929
Subject(s) - biology , histone methyltransferase , heterochromatin , histone code , histone h3 , histone , histone methylation , epigenomics , chromatin , ezh2 , histone modifying enzymes , genetics , bromodomain , nucleosome , histone h2a , histone h1 , heterochromatin protein 1 , microbiology and biotechnology , epigenetics , dna methylation , dna , gene , gene expression
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.

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