Automethylation activities within the mixed lineage leukemia-1 (MLL1) core complex reveal evidence supporting a "two-active site" model for multiple histone H3 lysine 4 methylation

Anamika Patel, Valarie E. Vought, Stephen Swatkoski, Susan Viggiano, Benny Howard, Venkatasubramanian Dharmarajan, Kelsey E. Monteith, Gillian Kupakuwana, Kevin E. Namitz, Stephen A. Shinsky, Robert J. Cotter, Michael S. Cosgrove

Research output: Contribution to journalArticle

Abstract

Background: The MLL1 core complex mono-and dimethylates histone H3 lysine 4 (H3K4). Results: MLL1 automethylates a conserved cysteine residue in its active site cleft. Conclusion: MLL1 automethylation is inhibited by unmodified histone H3 but not by histones previously mono-, di-, or trimethylated at H3K4.

Original languageEnglish (US)
Pages (from-to)868-884
Number of pages17
JournalJournal of Biological Chemistry
Volume289
Issue number2
DOIs
StatePublished - Jan 10 2014

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Patel, A., Vought, V. E., Swatkoski, S., Viggiano, S., Howard, B., Dharmarajan, V., Monteith, K. E., Kupakuwana, G., Namitz, K. E., Shinsky, S. A., Cotter, R. J., & Cosgrove, M. S. (2014). Automethylation activities within the mixed lineage leukemia-1 (MLL1) core complex reveal evidence supporting a "two-active site" model for multiple histone H3 lysine 4 methylation. Journal of Biological Chemistry, 289(2), 868-884. https://doi.org/10.1074/jbc.M113.501064