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Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.


A stable complex containing MLL1 and MOF has been immunoaffinity purified from a human cell line that stably expresses an epitope-tagged WDR5 subunit. Stable interactions between MLL1 and MOF were confirmed by reciprocal immunoprecipitation, cosedimentation, and cotransfection analyses, and interaction sites were mapped to MLL1 C-terminal and MOF zinc finger domains. The purified complex has a robust MLL1-mediated histone methyltransferase activity that can effect mono-, di-, and trimethylation of H3 K4 and a MOF-mediated histone acetyltransferase activity that is specific for H4 K16. Importantly, both activities are required for optimal transcription activation on a chromatin template in vitro and on an endogenous MLL1 target gene, Hox a9, in vivo. These results indicate an activator-based mechanism for joint MLL1 and MOF recruitment and targeted methylation and acetylation and provide a molecular explanation for the closely correlated distribution of H3 K4 methylation and H4 K16 acetylation on active genes.

Pubmed ID: 15960975


  • Dou Y
  • Milne TA
  • Tackett AJ
  • Smith ER
  • Fukuda A
  • Wysocka J
  • Allis CD
  • Chait BT
  • Hess JL
  • Roeder RG



Publication Data

June 17, 2005

Associated Grants


Mesh Terms

  • Acetyltransferases
  • DNA-Binding Proteins
  • HeLa Cells
  • Histone Acetyltransferases
  • Histone-Lysine N-Methyltransferase
  • Homeodomain Proteins
  • Humans
  • Microfilament Proteins
  • Multienzyme Complexes
  • Myeloid-Lymphoid Leukemia Protein
  • Proto-Oncogenes
  • Transcription Factors
  • Zinc Fingers