title: Different types of maize histone deacetylases are distinguished by a highly complex substrate and site specificity.
abstract: Enzymes involved in histone acetylation have been identified as important transcriptional regulators. Maize embryos contain three histone deacetylase families: RPD3-type deacetylases (HD1-B), nucleolar phosphoproteins of the HD2 family, and a third form unrelated to RPD3 and HD2 (HD1-A). Here we first report on the specificity of deacetylases for core histones, acetylated histone H4 subspecies, and acetylated H4-lysine residues. HD1-A, HD1-B, and HD2 deacetylate all four core histones, although with different specificity. However, experiments with histones from different sources (hyperacetylated MELC and chicken histones) using antibodies specific for individually acetylated H4-lysine sites indicate that the enzymes recognize highly distinct acetylation patterns. Only RPD3-type deacetylase HD1-B is able to deacetylate the specific H4 di-acetylation pattern (position 12 and 5) introduced by the purified cytoplasmic histone acetyltransferase B after incubation with pure nonacetylated H4 subspecies. HD1-A and HD2 exist as phosphorylated forms. Dephosphorylation has dramatic, but opposite effects; whereas HD2 loses enzymatic activity upon dephosphorylation, HD1-A is activated with a change of specificity against acetylated H4 subspecies. The data suggest that different types of deacetylases interact with different and highly specific acetylation patterns on nucleosomes.
authors.affiliation: Department of Microbiology, University of Innsbruck, Medical School, Austria.
authors.forename: D
authors.initials: D
authors.lastname: Kölle
authors.forename: G
authors.initials: G
authors.lastname: Brosch
authors.forename: T
authors.initials: T
authors.lastname: Lechner
authors.forename: A
authors.initials: A
authors.lastname: Pipal
authors.forename: W
authors.initials: W
authors.lastname: Helliger
authors.forename: J
authors.initials: J
authors.lastname: Taplick
authors.forename: P
authors.initials: P
authors.lastname: Loidl
mesh_terms: D000107:Acetylation; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D006655:Histone Deacetylases / Q000097:blood / Q000737:chemistry* / Q000378:metabolism*; D006657:Histones / Q000097:blood / Q000737:chemistry / Q000378:metabolism; D007527:Isoenzymes / Q000097:blood / Q000737:chemistry / Q000378:metabolism; D051379:Mice; D010766:Phosphorylation; D012156:Reticulocytes / Q000201:enzymology; D013379:Substrate Specificity; D014407:Tumor Cells, Cultured; D003313:Zea mays / Q000201:enzymology*
chemical_list: D006657:Histones; D007527:Isoenzymes; D006655:Histone Deacetylases