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Site-Specific Installation of Succinyl Lysine Analog into Histones Reveals the Effect of H2BK34 Succinylation on Nucleosome Dynamics
Cell Chemical Biology ( IF 8.6 ) Pub Date : 2017-12-14 , DOI: 10.1016/j.chembiol.2017.11.005
Yihang Jing , Zheng Liu , Gaofei Tian , Xiucong Bao , Toyotaka Ishibashi , Xiang David Li

Posttranslational modifications of histones play key roles in the dynamic regulation of chromatin structure. Lysine succinylation is a new type of histone modification, but its biological significance in chromatin structure and dynamics remains unknown. Here we develop a chemical approach to site-specifically install a succinyl lysine analog into histones. This analog serves as an ideal structural and functional mimic to natural succinyl lysine. The incorporation of this succinylation mimic into histone H2B at lysine 34, a succinylation site at the nucleosomal DNA-histone interface, leads to significant decrease in nucleosome stabilityin vitro, which is consistent with the defects in chromatin structure of a budding yeast strain containing a lysine-to-glutamate mutation at the corresponding residue of yeast histone H2B. This study provides a simple method for the rapid generation of histones with site-specific succinylation mimics, and reveals novel regulatory mechanisms of histone succinylation in the dynamic organization of chromatin.

中文翻译:

特定位置的琥珀酰赖氨酸类似物在组蛋白中的特定位置安装揭示了H2BK34琥珀酰化对核小体动力学的影响

组蛋白的翻译后修饰在染色质结构的动态调节中起关键作用。赖氨酸琥珀酰化是一种新型的组蛋白修饰,但其在染色质结构和动力学方面的生物学意义仍然未知。在这里,我们开发了一种化学方法,可以将琥珀酰赖氨酸类似物特异性地安装到组蛋白中。该类似物可作为天然琥珀酰赖氨酸的理想结构和功能模拟物。将此琥珀酰化模拟物掺入到赖氨酸34的组蛋白H2B中,赖氨酸34是核小体DNA-组蛋白界面的琥珀酰化位点,导致体外核小体稳定性显着降低,这与含有赖氨酸的发芽酵母菌株的染色质结构缺陷一致酵母组蛋白H2B相应残基的谷氨酸突变。
更新日期:2018-02-15
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