title: ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation.
abstract: ALL-1 is a member of the human trithorax/Polycomb gene family and is also involved in acute leukemia. ALL-1 is present within a stable, very large multiprotein supercomplex composed of > or =29 proteins. The majority of the latter are components of the human transcription complexes TFIID (including TBP), SWI/SNF, NuRD, hSNF2H, and Sin3A. Other components are involved in RNA processing or in histone methylation. The complex remodels, acetylates, deacetylates, and methylates nucleosomes and/or free histones. The complex's H3-K4 methylation activity is conferred by the ALL-1 SET domain. Chromatin immunoprecipitations show that ALL-1 and other complex components examined are bound at the promoter of an active ALL-1-dependent Hox a9 gene. In parallel, H3-K4 is methylated, and histones H3 and H4 are acetylated at this promoter.
authors.affiliation: Kimmel Cancer Center and Department of Microbiology, Jefferson Medical College, Philadelphia, PA 19107, USA. t_nakamura@mail.jci.tju.edu
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Nakamura
authors.forename: Toshiki
authors.initials: T
authors.lastname: Mori
authors.forename: Shinichiro
authors.initials: S
authors.lastname: Tada
authors.forename: Wladyslaw
authors.initials: W
authors.lastname: Krajewski
authors.forename: Tanya
authors.initials: T
authors.lastname: Rozovskaia
authors.forename: Richard
authors.initials: R
authors.lastname: Wassell
authors.forename: Garrett
authors.initials: G
authors.lastname: Dubois
authors.forename: Alexander
authors.initials: A
authors.lastname: Mazo
authors.forename: Carlo M
authors.initials: CM
authors.lastname: Croce
authors.forename: Eli
authors.initials: E
authors.lastname: Canaani
mesh_terms: D015153:Blotting, Western; D002467:Cell Nucleus / Q000378:metabolism; D002843:Chromatin / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D006367:HeLa Cells; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000378:metabolism; D018398:Homeodomain Proteins / Q000378:metabolism; D006801:Humans; D020014:K562 Cells; D013058:Mass Spectrometry; D008745:Methylation; D008780:Methyltransferases / Q000737:chemistry* / Q000378:metabolism; D051788:Myeloid-Lymphoid Leukemia Protein; D011233:Precipitin Tests; D011485:Protein Binding; D011496:Protein Methyltransferases; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D011519:Proto-Oncogenes; D016622:Silver Staining; D014157:Transcription Factors; D014158:Transcription, Genetic
chemical_list: D002843:Chromatin; D004268:DNA-Binding Proteins; D006657:Histones; D018398:Homeodomain Proteins; C497422:KMT2A protein, human; D014157:Transcription Factors; C097899:homeobox protein HOXA9; D051788:Myeloid-Lymphoid Leukemia Protein; D000076983:Histone Methyltransferases; D008780:Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase