Post-translational modifications of histones H3 and H4 associated with the histone methyltransferases Suv39h1 and G9a.
Specific combinations of post-translational modifications of histones alter chromatin structure, facilitating gene transcription or silencing. Here we have investigated the 'histone code' associated with the histone methyltransferases Suv39h1 and G9a by combining double immunopurification and mass spectrometry. Our results confirm the previously reported histone modifications associated with Suv39h1 and G9a. Moreover, this method allowed us to demonstrate for the first time an association of acetylated histones with the repressor proteins Suv39h1 and G9a.
Robin
Philippe
P
Centre National de la Recherche Scientifique (CNRS) FRE 2944, Institut André Lwoff, rue Guy Moquet, Villejuif F-94801, France. robin@vjf.cnrs.fr
Fritsch
Lauriane
L
Philipot
Ophélie
O
Svinarchuk
Fedor
F
Ait-Si-Ali
Slimane
S
D000107:Acetylation; D047369:Chromatin Immunoprecipitation; D006367:HeLa Cells; D006649:Histocompatibility Antigens / Q000378:metabolism*; D042421:Histone Code; D011495:Histone-Lysine N-Methyltransferase / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008780:Methyltransferases / Q000378:metabolism*; D009369:Neoplasms / Q000378:metabolism; D040901:Proteomics; D012097:Repressor Proteins / Q000378:metabolism*
D006649:Histocompatibility Antigens; D006657:Histones; D012097:Repressor Proteins; C407843:SUV39H1 protein, human; D008780:Methyltransferases; C445405:EHMT2 protein, human; D011495:Histone-Lysine N-Methyltransferase