• The Arabidopsis (ASHH2) CW domain binds monomethylated K4 of the histone H3 tail through conformational selection 

      Dobrovolska, Olena; Brilkov, Maxim; Madeleine, Noëlly; Ødegaard-Fougner, Øyvind; Strømland, Øyvind; Martin, Stephen R.; De Marco, Valeria; Christodoulou, Evangelos; Teigen, Knut; Isaksson, Johan; Underhaug, Jarl; Reuter, Nathalie; Aalen, Reidunn B.; Aasland, Rein; Halskau, Øyvind (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-02-21)
      Chromatin post‐translational modifications are thought to be important for epigenetic effects on gene expression. Methylation of histone N‐terminal tail lysine residues constitutes one of many such modifications, executed by families of histone lysine methyltransferase (HKMTase). One such protein is ASHH2 from the flowering plant <i>Arabidopsis thaliana</i>, equipped with the interaction domain, CW, ...
    • Binding Specificity of ASHH2 CW Domain Toward H3K4me1 Ligand Is Coupled to Its Structural Stability Through Its α1-Helix 

      Bril'kov, Maxim; Dobrovolska, Olena; Ødegård-Fougner, Øyvind; Turcu, Diana Cornelia; Strømland, Øyvind; Underhaug, Jarl; Aasland, Rein; Halskau, Øyvind (Journal article; Tidsskriftartikkel; Peer reviewed, 2022-04-13)
      The CW domain binds to histone tail modifications found in different protein families involved in epigenetic regulation and chromatin remodeling. CW domains recognize the methylation state of the fourth lysine on histone 3 and could, therefore, be viewed as a reader of epigenetic information. The specificity toward different methylation states such as me1, me2, or me3 depends on the particular ...