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

Zhipeng A WangSamuel D WhedonMingxuan WuSiyu WangEdward A BrownAnanya AnmangandlaLiam ReganKwangwoon LeeJianfeng DuJun Young HongLouise FairallTaylor KayHening LinYingming ZhaoJohn W R SchwabePhilip A Cole

Published in: Journal of the American Chemical Society (2022)

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.

Keyphrases

histone deacetylase
dna damage
gene expression
transcription factor
genome wide
atomic force microscopy
oxidative stress
mass spectrometry
high speed