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

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 ID: 12453419


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


Molecular cell

Publication Data

November 27, 2002

Associated Grants

  • Agency: NCI NIH HHS, Id: CA 50507

Mesh Terms

  • Blotting, Western
  • Cell Nucleus
  • Chromatin
  • DNA-Binding Proteins
  • HeLa Cells
  • Histone-Lysine N-Methyltransferase
  • Histones
  • Homeodomain Proteins
  • Humans
  • K562 Cells
  • Mass Spectrometry
  • Methylation
  • Methyltransferases
  • Myeloid-Lymphoid Leukemia Protein
  • Precipitin Tests
  • Protein Binding
  • Protein Methyltransferases
  • Protein Processing, Post-Translational
  • Protein Structure, Tertiary
  • Proto-Oncogenes
  • Silver Staining
  • Transcription Factors
  • Transcription, Genetic