Jmjd2b antagonizes H3K9 trimethylation at pericentric heterochromatin in mammalian cells.
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.
Fodor
Barna D
BD
Research Institute of Molecular Pathology (IMP), The Vienna Biocenter, A-1030 Vienna, Austria.
Kubicek
Stefan
S
Yonezawa
Masato
M
O'Sullivan
Roderick J
RJ
Sengupta
Roopsha
R
Perez-Burgos
Laura
L
Opravil
Susanne
S
Mechtler
Karl
K
Schotta
Gunnar
G
Jenuwein
Thomas
T
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
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