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

Autor:	Zhipeng A. Wang, Samuel D. Whedon, Mingxuan Wu, Siyu Wang, Edward A. Brown, Ananya Anmangandla, Liam Regan, Kwangwoon Lee, Jianfeng Du, Jun Young Hong, Louise Fairall, Taylor Kay, Hening Lin, Yingming Zhao, John W. R. Schwabe, Philip A. Cole
Rok vydání:	2022
Předmět:	Histones Colloid and Surface Chemistry Sirtuins General Chemistry Biochemistry Chromatin Histone Deacetylases Catalysis Nucleosomes
Zdroj:	Journal of the American Chemical Society. 144:3360-3364
ISSN:	1520-5126 0002-7863
DOI:	10.1021/jacs.1c13555
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3b42f643da4cea27457c1d37bbc02ee https://doi.org/10.1021/jacs.1c13555 Zobrazit plný text záznamu