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ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation.

Authors :
Nakamura T
Mori T
Tada S
Krajewski W
Rozovskaia T
Wassell R
Dubois G
Mazo A
Croce CM
Canaani E
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.

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