Abstract
Holocarboxylase synthetase (HCS) catalyzes the covalent binding of biotin to lysine (K) residues in histones. Histone biotinylation is biologically important for gene regulation in humans. For example, biotinylation of the K‐12 in histone H4 (H4K12bio) represses the transcription of genes coding for transposable elements, interleukin‐2, and the sodium‐dependent multivitamin transporter. Mass spectrometry studies provided preliminary evidence for the existence of a novel biotinylation site, H4K16bio, in addition to the 11 known biotinylation sites in histones H2A, H3 and H4. In this study we developed a new antibody to H4K16bio and conducted an extensive series of tests to confirm specificity. Bulk extracts of human histones tested positive for H4K16bio, using the novel antibody as a probe. Currently, we are using ChIP/qRT‐PCR to obtain first insights into potential biological functions of H4K16bio. (Supported by ARD, NIH DK063945, DK077816, DK082476 and ES015206, USDA CSREES 2006‐35200‐17138, and NSF EPS 070189).
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