title: Expanding the Reader Landscape of Histone Acylation.
abstract: In this issue of Structure,Klein et al. (2017) expand our understanding of what reader domains bind to by showing that MORF, a double PHD domain containing lysine acetyltransferase, is a preferential reader of histone lysine acylation.
authors.affiliation: Department of Biochemistry and Biophysics, The University of North Carolina, Chapel Hill, NC 27599, USA; Lineberger Comprehensive Cancer Center, The University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
authors.forename: Abid
authors.initials: A
authors.lastname: Khan
authors.affiliation: Department of Biochemistry and Biophysics, The University of North Carolina, Chapel Hill, NC 27599, USA; Lineberger Comprehensive Cancer Center, The University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
authors.forename: Joseph B
authors.initials: JB
authors.lastname: Bridgers
authors.affiliation: Department of Biochemistry and Biophysics, The University of North Carolina, Chapel Hill, NC 27599, USA; Lineberger Comprehensive Cancer Center, The University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA. Electronic address: brian_strahl@med.unc.edu.
authors.forename: Brian D
authors.initials: BD
authors.lastname: Strahl
mesh_terms: D000215:Acylation; D051548:Histone Acetyltransferases / Q000737:chemistry; D006657:Histones / Q000737:chemistry*; D008239:Lysine
chemical_list: D006657:Histones; D051548:Histone Acetyltransferases; D008239:Lysine