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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.

Original publication

DOI

10.1016/j.cell.2005.04.031

Type

Journal article

Journal

Cell

Publication Date

17/06/2005

Volume

121

Pages

873 - 885

Keywords

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