Histone H2B Deacylation Selectivity: Exploring Chromatin's Dark Matter with an Engineered Sortase

J Am Chem Soc. 2022 Mar 2;144(8):3360-3364. doi: 10.1021/jacs.1c13555. Epub 2022 Feb 17.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatin
  • Histone Deacetylases / genetics
  • Histones* / chemistry
  • Nucleosomes
  • Sirtuins*

Substances

  • Chromatin
  • Histones
  • Nucleosomes
  • Sirtuins
  • Histone Deacetylases