Chemically synthesized histone H2A Lys13 di-ubiquitination promotes binding of 53BP1 to nucleosomes

摘要：

Dear Editor,p53-binding protein 1 (53BP1) is a critical regulator of cellular response to DNA double-strand breaks (DSBs) ”1”.To accomplish its repair function,53BP1 must be recruited to the chromatin surrounding DSB sites that carry H4 methylation at Lys20 and H2A ubiquitination at Lysl5 ”2-5”.The structural basis of this recognition process was recently revealed by the complex structure of 53BP1 bound to a nucleosome core particle (NCP) containing Lys20-dimethylated H4 (H4K20me2) and Lysl5-mono-ubiquitinated H2A (H2AK15monoUb) ”6”.It is fascinating to note that ubiquitin ligase RNF168 ubiquitinated H2A not only on Lysl5,but also on Lysl3 without selectivity,and H2A bearing the K15Q mutation was still poly-ubiquitinated at Lysl3 in vivo ”2-4,7”.

所属期刊栏目：28

资助基金：We thank Drs Rui-Ming Xu and Qing-Long You Institute of Biophysics,Chinese Academy of Sciences for kindly providing the GST-53BP1 plasmid.We also thank the Center for Biomedical Analysis of Tsinghua University for sample analysis.This work was supported by the National Key Research and Development2017YFA0505200 and 2016YFA0400903;the National Natural Science Foundation of China21532004,81621002,21621003and 21708036

在线出版日期：2018-04-04（万方平台首次上网日期，不代表论文的发表时间）

页数：共4页

页码：257-260