半合成泛素化组蛋白H2A揭示了去泛素化酶的不同活性以及组蛋白H2A赖氨酸119位泛素化对单核小体中组蛋白H3赖氨酸36位甲基化的抑制作用。
Semisynthetic UbH2A reveals different activities of deubiquitinases and inhibitory effects of H2A K119 ubiquitination on H3K36 methylation in mononucleosomes.
作者信息
Bi Xiaobao, Yang Renliang, Feng Xiaoyu, Rhodes Daniela, Liu Chuan-Fa
机构信息
Division of Structural Biology and Biochemistry, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.
出版信息
Org Biomol Chem. 2016 Jan 21;14(3):835-9. doi: 10.1039/c5ob02323h. Epub 2015 Nov 30.
Using a genetically incorporated azidonorleucine for ubiquitin installation, we prepared multi-milligram quantities of H2AK119ub (ubH2A). With a native isopeptide linkage, the synthetic ubH2A was used to study the activity of deubiquitinases and crosstalk between H2A ubiquitination and H3K36 methylation in the context of chemically defined mononucleosomes.
我们利用基因编码的叠氮亮氨酸进行泛素化修饰，制备了多毫克量的H2AK119泛素化组蛋白（ubH2A）。该合成的ubH2A具有天然的异肽键，用于在化学定义的单核小体背景下研究去泛素化酶的活性以及H2A泛素化与H3K36甲基化之间的相互作用。
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