title: Methylation of histone H3 lysine 9 occurs during translation.
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.
authors.affiliation: Fundación Ciencia & Vida, 7780272, Santiago, Chile.
authors.forename: Carlos
authors.initials: C
authors.lastname: Rivera
authors.affiliation: Fundación Ciencia & Vida, 7780272, Santiago, Chile.
authors.forename: Francisco
authors.initials: F
authors.lastname: Saavedra
authors.affiliation: Fundación Ciencia & Vida, 7780272, Santiago, Chile.
authors.forename: Francisca
authors.initials: F
authors.lastname: Alvarez
authors.affiliation: Fundación Ciencia & Vida, 7780272, Santiago, Chile.
authors.forename: César
authors.initials: C
authors.lastname: Díaz-Celis
authors.affiliation: Fundación Ciencia & Vida, 7780272, Santiago, Chile.
authors.forename: Valentina
authors.initials: V
authors.lastname: Ugalde
authors.affiliation: Munich Center of Integrated Protein Science and Adolf-Butenandt Institute, 80336 Muenchen, Germany.
authors.forename: Jianhua
authors.initials: J
authors.lastname: Li
authors.affiliation: Munich Center of Integrated Protein Science and Adolf-Butenandt Institute, 80336 Muenchen, Germany.
authors.forename: Ignasi
authors.initials: I
authors.lastname: Forné
authors.affiliation: 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.
authors.forename: Zachary A
authors.initials: ZA
authors.lastname: Gurard-Levin
authors.affiliation: 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.
authors.forename: Geneviève
authors.initials: G
authors.lastname: Almouzni
authors.affiliation: Munich Center of Integrated Protein Science and Adolf-Butenandt Institute, 80336 Muenchen, Germany.
authors.forename: Axel
authors.initials: A
authors.lastname: Imhof
authors.affiliation: Fundación Ciencia & Vida, 7780272, Santiago, Chile aloyola@cienciavida.org.
authors.forename: Alejandra
authors.initials: A
authors.lastname: Loyola
mesh_terms: D006367:HeLa Cells; D011495:Histone-Lysine N-Methyltransferase / Q000378:metabolism; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D008745:Methylation; D014176:Protein Biosynthesis; D011496:Protein Methyltransferases / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D012270:Ribosomes / Q000201:enzymology
chemical_list: D006657:Histones; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; C454062:SETDB1 protein, human; D008239:Lysine