Structural Analysis of the Ash2L/Dpy-30 Complex Reveals a Heterogeneity in H3K4 Methylation

John Faissal Haddad, Yidai Yang, Yoh hei Takahashi, Monika Joshi, Nidhi Chaudhary, Ashley R. Woodfin, Aissa Benyoucef, Sylvain Yeung, Joseph S. Brunzelle, Georgios Skiniotis, Marjorie Brand, Ali Shilatifard, Jean François Couture*

*Corresponding author for this work

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

Haddad et al. highlight that several interactions help in the formation of the Ash2L/Dpy-30 complex. The study also demonstrates that Dpy-30 couples its marginal ability to allosterically regulate KMT2 enzymes and chromatin recruitment activity to control epigenetic signaling in vivo.

Original languageEnglish (US)
Pages (from-to)1594-1603.e4
JournalStructure
Volume26
Issue number12
DOIs
StatePublished - Dec 4 2018

Keywords

  • H3K4 methylation
  • KMT2
  • MLL
  • SET1/COMPASS
  • allosteric regulation
  • chromatin
  • crystallography
  • histone
  • lysine methylation

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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  • Cite this

    Haddad, J. F., Yang, Y., Takahashi, Y. H., Joshi, M., Chaudhary, N., Woodfin, A. R., Benyoucef, A., Yeung, S., Brunzelle, J. S., Skiniotis, G., Brand, M., Shilatifard, A., & Couture, J. F. (2018). Structural Analysis of the Ash2L/Dpy-30 Complex Reveals a Heterogeneity in H3K4 Methylation. Structure, 26(12), 1594-1603.e4. https://doi.org/10.1016/j.str.2018.08.004