title: The role of holocarboxylase synthetase in genome stability is mediated partly by epigenomic synergies between methylation and biotinylation events.
abstract: Holocarboxylase synthetase (HLCS) catalyzes the covalent binding of biotin to histones. Biotinylated histones are gene repression marks and are particularly enriched in long terminal repeats, telomeres, and other repeat regions. The effects of HLCS in gene regulation are mediated by its physical interactions with chromatin proteins such as histone H3, DNMT1, MeCP2, and EHMT-1. It appears that histone biotinylation depends on prior methylation of cytosines. De-repression of long terminal repeats in biotin- or HLCS-deficient cell cultures and organisms is associated with genome instability.
authors.affiliation: Department of Nutrition and Health Sciences, University of Nebraska-Lincoln, Lincoln, NE, USA. jzempleni2@unl.edu
authors.forename: Janos
authors.initials: J
authors.lastname: Zempleni
authors.forename: Yong
authors.initials: Y
authors.lastname: Li
authors.forename: Jing
authors.initials: J
authors.lastname: Xue
authors.forename: Elizabeth L
authors.initials: EL
authors.lastname: Cordonier
mesh_terms: D019921:Biotinylation / Q000235:genetics; D019731:Carbon-Nitrogen Ligases / Q000235:genetics* / Q000378:metabolism*; D044127:Epigenesis, Genetic; D015870:Gene Expression; D016678:Genome / Q000235:genetics*; D042822:Genomic Instability / Q000235:genetics*; D006657:Histones / Q000378:metabolism; D028922:Holocarboxylase Synthetase Deficiency / Q000235:genetics; D008745:Methylation; D010641:Phenotype
chemical_list: D006657:Histones; D019731:Carbon-Nitrogen Ligases; C023312:holocarboxylase synthetases