Crystal structure of the trithorax group protein ASH2L reveals a forkhead-like DNA binding domain

Sabina Sarvan, Vanja Avdic, Veronique Tremblay, Chandra Prakash Chaturvedi, Pamela Zhang, Sylvain Lanouette, Alexandre Blais, Joseph S. Brunzelle, Marjorie Brand, Jean François Couture*

*Corresponding author for this work

Research output: Contribution to journalArticle

30 Scopus citations

Abstract

Absent, small or homeotic discs-like 2 (ASH2L) is a trithorax group (TrxG) protein and a regulatory subunit of the SET1 family of lysine methyltransferases. Here we report that ASH2L binds DNA using a forkhead-like helix-wing-helix (HWH) domain. In vivo, the ASH2L HWH domain is required for binding to the -globin locus control region, histone H3 Lys4 (H3K4) trimethylation and maximal expression of the globin gene (Hbb-1), validating the functional importance of the ASH2L DNA binding domain.

Original languageEnglish (US)
Pages (from-to)857-859
Number of pages3
JournalNature Structural and Molecular Biology
Volume18
Issue number7
DOIs
StatePublished - Jul 1 2011

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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    Sarvan, S., Avdic, V., Tremblay, V., Chaturvedi, C. P., Zhang, P., Lanouette, S., Blais, A., Brunzelle, J. S., Brand, M., & Couture, J. F. (2011). Crystal structure of the trithorax group protein ASH2L reveals a forkhead-like DNA binding domain. Nature Structural and Molecular Biology, 18(7), 857-859. https://doi.org/10.1038/nsmb.2093