Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2002-11-27
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Histone-Lysine N-Methyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/Histones, http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins, http://linkedlifedata.com/resource/pubmed/chemical/MLL protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Methyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Myeloid-Lymphoid Leukemia Protein, http://linkedlifedata.com/resource/pubmed/chemical/Protein Methyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/histone methyltransferase, http://linkedlifedata.com/resource/pubmed/chemical/homeobox protein HOXA9
pubmed:status
MEDLINE
pubmed:author
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1119-28
pubmed:dateRevised
2008-11-21
pubmed:articleTitle
ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation.
pubmed:affiliation
Kimmel Cancer Center and Department of Microbiology, Jefferson Medical College, Philadelphia, PA 19107, USA. t_nakamura@mail.jci.tju.edu