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

被引:566
作者
Nakamura, T [1 ]
Mori, T
Tada, S
Krajewski, W
Rozovskaia, T
Wassell, R
Dubois, G
Mazo, A
Croce, CM
Canaani, E
机构
[1] Thomas Jefferson Univ, Coll Med, Kimmel Canc Ctr, Philadelphia, PA 19107 USA
[2] Thomas Jefferson Univ, Coll Med, Dept Microbiol, Philadelphia, PA 19107 USA
[3] Weizmann Inst Sci, Dept Mol Cell Biol, IL-76100 Rehovot, Israel
关键词
D O I
10.1016/S1097-2765(02)00740-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 greater than or equal to29 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 histories H3 and H4 are acetylated at this promoter.
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收藏
页码:1119 / 1128
页数:10
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