Molecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes

Melissa M. Steward, Jung Shin Lee, Aisling O'Donovan, Matt Wyatt, Bradley E. Bernstein, Ali Shilatifard*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

233 Scopus citations

Abstract

MLL complexes are homologs of yeast COMPASS capable of methylating histone H3 Lys4 (H3K4). ASH2L, RbBP5 and WDR5 are conserved subunits of MLL complexes with homology to the Cps40/Cps60, Cps50 and Cps30 subunits of COMPASS, respectively. We report that ASH2L differentially regulates MLL's catalysis of H3K4 trimethylation similarly to Cps40 and Cps60. Furthermore, WDR5 is required to maintain MLL complex integrity, including the stability of ASH2L within the complex. These findings offer insight into the molecular role of ASH2L, and by extension that of WDR5, in proper H3K4 trimethylation.

Original languageEnglish (US)
Pages (from-to)852-854
Number of pages3
JournalNature Structural and Molecular Biology
Volume13
Issue number9
DOIs
StatePublished - Sep 2006

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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