title: Jmjd2b antagonizes H3K9 trimethylation at pericentric heterochromatin in mammalian cells.
abstract: Histone lysine trimethyl states represent some of the most robust epigenetic modifications in eukaryotic chromatin. Using a candidate approach, we identified the subgroup of murine Jmjd2 proteins to antagonize H3K9me3 at pericentric heterochromatin. H3K27me3 and H4K20me3 marks are not impaired in inducible Jmjd2b-GFP cell lines, but Jmjd2b also reduces H3K36 methylation. Since recombinant Jmjd2b appears as a very poor enzyme, we applied metabolic labeling with heavy methyl groups to demonstrate Jmjd2b-mediated removal of chromosomal H3K9me3 as an active process that occurs well before replication of chromatin. These data reveal that certain members of the jmjC class of hydroxylases can work in a pathway that actively antagonizes a histone lysine trimethyl state.
authors.affiliation: Research Institute of Molecular Pathology (IMP), The Vienna Biocenter, A-1030 Vienna, Austria.
authors.forename: Barna D
authors.initials: BD
authors.lastname: Fodor
authors.forename: Stefan
authors.initials: S
authors.lastname: Kubicek
authors.forename: Masato
authors.initials: M
authors.lastname: Yonezawa
authors.forename: Roderick J
authors.initials: RJ
authors.lastname: O'Sullivan
authors.forename: Roopsha
authors.initials: R
authors.lastname: Sengupta
authors.forename: Laura
authors.initials: L
authors.lastname: Perez-Burgos
authors.forename: Susanne
authors.initials: S
authors.lastname: Opravil
authors.forename: Karl
authors.initials: K
authors.lastname: Mechtler
authors.forename: Gunnar
authors.initials: G
authors.lastname: Schotta
authors.forename: Thomas
authors.initials: T
authors.lastname: Jenuwein
mesh_terms: D000818:Animals; D002478:Cells, Cultured; D033481:Chromosomes, Mammalian / Q000235:genetics; D006570:Heterochromatin / Q000235:genetics / Q000378:metabolism*; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D056484:Jumonji Domain-Containing Histone Demethylases; D008239:Lysine / Q000378:metabolism; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism; D051379:Mice; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000378:metabolism*; D009363:Neoplasm Proteins / Q000737:chemistry / Q000378:metabolism*; D012097:Repressor Proteins / Q000378:metabolism
chemical_list: D006570:Heterochromatin; D006657:Histones; D009363:Neoplasm Proteins; D012097:Repressor Proteins; D006899:Mixed Function Oxygenases; D056484:Jumonji Domain-Containing Histone Demethylases; C511781:Kdm4b protein, mouse; C498700:Suv39h1 protein, mouse; D008780:Methyltransferases; D008239:Lysine