组蛋白 H2B 去乙酰化选择性：用工程化的 sortase 探索染色质的暗物质。
Histone H2B Deacylation Selectivity: Exploring Chromatin's Dark Matter with an Engineered Sortase.
机构信息
Division of Genetics, Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts 02115, United States.
Department of Biological Chemistry and Molecular Pharmcology, Harvard Medical School, Boston, Massachusetts 02115, United States.
出版信息
J Am Chem Soc. 2022 Mar 2;144(8):3360-3364. doi: 10.1021/jacs.1c13555. Epub 2022 Feb 17.
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.
我们描述了一种通过半合成利用工程化的 sortase 转肽酶产生组蛋白 H2B 的新方法。N-末端尾部特异性修饰的乙酰化、乳酰化和β-羟基丁酰化组蛋白 H2B 被掺入核小体中，并作为组蛋白去乙酰化酶（HDAC）复合物和 Sirtuins 的底物进行研究。这些酶形式观察到的速率和特异性范围很广，表明它们在调节染色质结构和表观遗传学方面具有不同的生物学作用。
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