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Molecular, Genetic, and Biochemical Nutrition Commons

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Department of Nutrition and Health Sciences: Dissertations, Theses, and Student Research

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Biotin; histone; holocarboxylase synthetase; human

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Full-Text Articles in Molecular, Genetic, and Biochemical Nutrition

Holocarboxylase Synthetase-Dependent Biotinylation Of Histone H4, Luisa F. Rios Avila Jul 2010

Holocarboxylase Synthetase-Dependent Biotinylation Of Histone H4, Luisa F. Rios Avila

Department of Nutrition and Health Sciences: Dissertations, Theses, and Student Research

Holocarboxylase synthetase (HCS) catalyzes the binding of biotin to lysine (K) residues in histones H3 and H4. Histone biotinylation marks play important roles in the repression of genes and retrotransposons. Preliminary studies suggested that K16 in histone H4 is a target for biotinylation by HCS. Here we demonstrated that H4K16bio is overrepresented in repeat regions {pericentromeric alpha satellite repeats; long terminal repeats (LTR)} compared with euchromatin promoters. H4K16bio was also enriched in the repressed interleukin-2 gene promoter. The enrichment at LTR22 and promoter 1 of the sodium-dependent multivitamin transporter (SMVT) depended on biotin supply; and was significantly lower in fibroblasts …