Back to Search
Start Over
ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation.
- Source :
-
Molecular cell [Mol Cell] 2002 Nov; Vol. 10 (5), pp. 1119-28. - Publication Year :
- 2002
-
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.
- Subjects :
- Blotting, Western
Cell Nucleus metabolism
Chromatin metabolism
DNA-Binding Proteins chemistry
HeLa Cells
Histone Methyltransferases
Histones metabolism
Homeodomain Proteins metabolism
Humans
K562 Cells
Mass Spectrometry
Methylation
Methyltransferases metabolism
Myeloid-Lymphoid Leukemia Protein
Precipitin Tests
Protein Binding
Protein Methyltransferases
Protein Processing, Post-Translational
Protein Structure, Tertiary
Silver Staining
DNA-Binding Proteins metabolism
Histone-Lysine N-Methyltransferase
Methyltransferases chemistry
Proto-Oncogenes
Transcription Factors
Transcription, Genetic
Subjects
Details
- Language :
- English
- ISSN :
- 1097-2765
- Volume :
- 10
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Molecular cell
- Publication Type :
- Academic Journal
- Accession number :
- 12453419
- Full Text :
- https://doi.org/10.1016/s1097-2765(02)00740-2