Abstract
We describe a new method to produce histone H2B by semisynthesis with an engineered sortase transpeptidase. N-Terminal tail site-specifically modified acetylated, lactylated, and β-hydroxybutyrylated histone H2Bs were incorporated into nucleosomes and investigated as substrates of histone deacetylase (HDAC) complexes and sirtuins. A wide range of rates and site-specificities were observed by these enzyme forms suggesting distinct biological roles in regulating chromatin structure and epigenetics.
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CITATION STYLE
Wang, Z. A., Whedon, S. D., Wu, M., Wang, S., Brown, E. A., Anmangandla, A., … Cole, P. A. (2022). Histone H2B Deacylation Selectivity: Exploring Chromatin’s Dark Matter with an Engineered Sortase. Journal of the American Chemical Society, 144(8), 3360–3364. https://doi.org/10.1021/jacs.1c13555
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