title: Diverse ways to be specific: a novel Zn-binding domain confers substrate specificity to UTX/KDM6A histone H3 Lys 27 demethylase.
abstract: Histone methylations are highly regulated by site-specific histone methyltransferases and demethylases. In this issue of Genes & Development, Sengoku and Yokoyama (pp. 2266-2277) demonstrate that a novel Zn-binding domain and the Jumonji domain of UTX/KDM6A (Lys demethylase 6A) recognize histone H3 and together function as a substrate specificity determinant for H3K27 demethylation. This study demonstrates the mechanism of site-specific demethylation by UTX/KDM6A and implicates that histone demethylases use diverse methods to accomplish target specificity.
authors: Department of Biological Sciences, Graduate School of Nanoscience and Technology (WCU), KAIST, Daejeon, South Korea.
authors: Eunji
authors: E
authors: Kim
authors: Ji-Joon
authors: JJ
authors: Song
mesh_terms: D000818:Animals; D056466:Histone Demethylases / Q000378:metabolism*; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D009687:Nuclear Proteins / Q000378:metabolism*
chemical_list: D006657:Histones; D009687:Nuclear Proteins; D056466:Histone Demethylases; C523998:KDM6A protein, human