Volume 24, No 7, Jul 2014

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

Volume 24 Issue 7, July 2014: 890-893

LETTERS TO THE EDITOR

Crystal structure of human BS69 Bromo-ZnF-PWWP reveals its role in H3K36me3 nucleosome binding

Juncheng Wang¹, Su Qin¹, Fudong Li¹, Sai Li¹, Wei Zhang², Junhui Peng¹, Zhiyong Zhang¹, Qingguo Gong¹, Jihui Wu¹ and Yunyu Shi¹

¹Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China
²Biomedical Research Institute, Shenzhen-PKU-HKUST Medical Center, Shenzhen, Guangdong 518036, China Correspondence: Jihui Wu, E-mail: wujihui@ustc.edu.cn; Yunyu Shi, E-mail:(yyshi@ustc.edu.cn)

The eukaryotic genome is packed into highly compacted chromatin, the basic unit of which is a nucleosome composed of 147 base pairs of DNA wrapped around the histone octamer1. Post-translational modifications along histone N-terminal tails can be recognized by various 'reader' modules2. PWWP domain, one type of 'reader' modules, has been identified to recognize H3K36me3 in the peptide and nucleosome context3,4,5.

10.1038/cr.2014.38

FULL TEXT | PDF

Browse 2180