title: Linking genome structure and function through specific histone acetylation.
abstract: A recent publication shows that a simple chemical event, acetylation of lysine 16 on the histone H4 N-terminal tail domain (NTD), completely abolishes the ability of the H4 NTD to mediate the nucleosome-nucleosome interactions involved in chromatin condensation. This result provides novel insight into the molecular mechanism of histone acetylation and also implicates H4 K16acet-dependent changes in chromatin fiber architecture as a central mechanism for generating transcriptionally active genomic domains.
authors.affiliation: Department of Biochemistry and Molecular Biology, 1870 Campus Delivery, Colorado State University, Fort Collins, Colorado 80523, USA. jeffrey.c.hansen@colostate.edu
authors.forename: Jeffrey C
authors.initials: JC
authors.lastname: Hansen
mesh_terms: D000107:Acetylation; D006657:Histones / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D017434:Protein Structure, Tertiary
chemical_list: D006657:Histones