title: A novel, enigmatic histone modification: biotinylation of histones by holocarboxylase synthetase.
abstract: Holocarboxylase synthetase catalyzes the covalent binding of biotin to histones in humans and other eukaryotes. Eleven biotinylation sites have been identified in histones H2A, H3, and H4. K12-biotinylated histone H4 is enriched in heterochromatin, repeat regions, and plays a role in gene repression. About 30% of the histone H4 molecules are biotinylated at K12 in histone H4 in human fibroblast telomeres. The abundance of biotinylated histones at distinct genomic loci depends on biotin availability. Decreased histone biotinylation decreases life span and stress resistance in Drosophila. Low enrichment of biotinylated histones at transposable elements impairs repression of these elements.
authors.affiliation: Department of Nutrition and Health Sciences, University of Nebraska-Lincoln, Lincoln, Nebraska 68583-0806, USA.
authors.forename: Yousef I
authors.initials: YI
authors.lastname: Hassan
authors.forename: Janos
authors.initials: J
authors.lastname: Zempleni
mesh_terms: D000818:Animals; D001710:Biotin / Q000008:administration & dosage / Q000378:metabolism*; D019921:Biotinylation / Q000502:physiology*; D019731:Carbon-Nitrogen Ligases / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006801:Humans
chemical_list: D006657:Histones; D001710:Biotin; D019731:Carbon-Nitrogen Ligases; C023312:holocarboxylase synthetases