@inbook{11a95079689945c58f31ea09a62d6b23,
title = "Use of synthetic peptides for identifying biotinylation sites in human histones",
abstract = "Posttranslational modifications of histones play an important role in the regulation of chromatin structure and, hence, gene regulation. Recently, we have identified a novel modification of histones: binding of the vitamin biotin to lysine residues in histones H2A, H3, and H4. Here, we describe a procedure to identify those amino acids that are targets for biotinylation in histones. Briefly, the following analytical, sequence is used to identify biotinylation sites: (i) short peptides (<20 amino acids in length) are synthesized chemically; amino acid sequences in the peptides are based on the sequence in a given region of a given histone; (ii) peptides are incubated with biotinidase or holocarboxylase synthetase to conduct, enzymatic biotinylation; and (iii) biotin in peptides are probed using streptavidin peroxidase. Amino acid substitutions (e.g., lysine-to-alanine substitutions) in synthetic peptides can be used to corroborate identification of biotinylation sites.",
keywords = "Biotinidase, Biotinylation, Chromatin, Histones, Holocarboxylase",
author = "Gabriela Camporeale and Yap, {Ching Chew} and Alice Kueh and Gautam Sarath and Janos Zempleni",
year = "2007",
month = dec,
day = "15",
doi = "10.1385/1-59745-579-2:139",
language = "English (US)",
isbn = "9781597455794",
series = "Methods in Molecular Biology",
publisher = "Humana Press",
pages = "139--148",
booktitle = "Avidin-Biotin Interactions - Methods and Applications",
}