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United States Department of Agriculture-Agricultural Research Service / University of Nebraska-Lincoln: Faculty Publications
Biocytin; Biotin; Biotinidase; Histone H2A; Holocarboxylase synthetase; Lysine
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Lysine Residues In N-Terminal And C-Terminal Regions Of Human Histone H2a Are Targets For Biotinylation By Biotinidase, Yap Ching Chew, Gabreale Camporeale, Nagarama Kothapalli, Gautam Sarath, Janos Zempleni
Lysine Residues In N-Terminal And C-Terminal Regions Of Human Histone H2a Are Targets For Biotinylation By Biotinidase, Yap Ching Chew, Gabreale Camporeale, Nagarama Kothapalli, Gautam Sarath, Janos Zempleni
United States Department of Agriculture-Agricultural Research Service / University of Nebraska-Lincoln: Faculty Publications
In eukaryotic cell nuclei, DNA associates with the core histones H2A, H2B, H3 and H4 to form nucleosomal core particles. DNA binding to histones is regulated by posttranslational modifications of N-terminal tails (e.g., acetylation and methylation of histones). These modifications play important roles in the epigenetic control of chromatin structure. Recently, evidence that biotinidase and holocarboxylase synthetase (HCS) catalyze the covalent binding of biotin to histones has been provided. The primary aim of this study was to identify biotinylation sites in histone H2A and its variant H2AX. Secondary aims were to determine whether acetylation and methylation of histone H2A affect …