Regulation of MLL1 H3K4 methyltransferase activity by its core components.

Journal article

Histone H3 Lys4 (H3K4) methylation is a prevalent mark associated with transcription activation. A common feature of several H3K4 methyltransferase complexes is the presence of three structural components (RbBP5, Ash2L and WDR5) and a catalytic subunit containing a SET domain. Here we report the first biochemical reconstitution of a functional four-component mixed-lineage leukemia protein-1 (MLL1) core complex. This reconstitution, combined with in vivo assays, allows direct analysis of the c...

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Authors: Dou, Y; Milne, T; Ruthenburg, A; Lee, S; Lee, J

• Publication status: Published
• Journal: Nature structural and molecular biology
• Volume: 13
• Issue: 8
• Pages: 713-719
• Publication date: 2006-08-01
• DOI: 10.1038/nsmb1128
• EISSN: 1545-9985
• ISSN: 1545-9993
• Language: English
• Keywords: Recombinant Proteins; Histone-Lysine N-Methyltransferase; Myeloid-Lymphoid Leukemia Protein; DNA-Binding Proteins; RNA Interference; Cell Line; Nuclear Proteins; Lysine; Multiprotein Complexes; Transcription Factors; Methylation; Humans; Catalytic Domain; Histones; Heterotrimeric GTP-Binding Proteins