Volume 28, No 2, Feb 2018

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 28 Issue 2, February 2018: 262-262

ERRATUM

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

Jia-Bin Li^{1, *}, Yun-Kun Qi^{2, 3, *}, Qiao-Qiao He²,Hua-Song Ai², San-ling Liu¹, Jia-Xing Wang²,Ji-Shen Zheng¹, Lei Liu², Changlin Tian¹

¹Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, China;
²Tsinghua-Peking Center for Life Sciences, Department of Chemistry, Tsinghua University, Beijing 100084, China; 3School of Pharmacy, Qingdao University, Qingdao, Shandong 266021,China Correspondence: Changlin Tian(cltian@ustc.edu.cn)

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 Lys15 [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 Lys15-mono-ubiquitinated H2A (H2AK15monoUb) [6]. It is fascinating to note that ubiquitin ligase RNF168 ubiquitinated H2A not only on Lys15, but also on Lys13 without selectivity, and H2A bearing the K15Q mutation was still poly-ubiquitinated at Lys13 in vivo [2-4, 7]. This leads to two questions. First, is 53BP1 also a reader of H2A Lys13 ubiquitin mark? Second, is poly-ubiquitination redundant at the 53BP1 recruitment event?

10.1038/cr.2017.157

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