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. 2002 Nov;10(5):1119-28.
doi: 10.1016/s1097-2765(02)00740-2.

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

Tatsuya Nakamura  1 , Toshiki Mori, Shinichiro Tada, Wladyslaw Krajewski, Tanya Rozovskaia, Richard Wassell, Garrett Dubois, Alexander Mazo, Carlo M Croce, Eli Canaani
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Free article

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

Tatsuya Nakamura et al. Mol Cell. 2002 Nov.
Free article

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.

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