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Updated: Jun 1, 2026

Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
Published on: November 1, 2012
Crystal structure of the trithorax group protein ASH2L reveals a forkhead-like DNA binding domain
Sabina Sarvan1, Vanja Avdic, Véronique Tremblay
1Ottawa Institute of Systems Biology, Department of Biochemistry, University of Ottawa, Ottawa, Ontario, Canada.
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 β-globin locus control region, histone H3 Lys4 (H3K4) trimethylation and maximal expression of the β-globin gene (Hbb-1), validating the functional importance of the ASH2L DNA binding domain.
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