中科院上海药物研究所徐华强等研究人员合作揭示核小体结合的DNA甲基转移酶DNMT3A和DNMT3B结构。相关论文于2020年9月23日在线发表在《自然》杂志上。
Title: Structure of nucleosome-bound DNA methyltransferases DNMT3A and DNMT3B
Author: Ting-Hai Xu, Minmin Liu, X. Edward Zhou, Gangning Liang, Gongpu Zhao, H. Eric Xu, Karsten Melcher, Peter A. Jones
Issue&Volume: 2020-09-23
Abstract: CpG methylation by de novo DNA methyltransferases (DNMTs) 3A and 3B is essential for mammalian development and differentiation and is frequently dysregulated in cancer1. These two DNMTs preferentially bind to nucleosomes, yet cannot methylate the DNA wrapped around the nucleosome core2, and they favour the methylation of linker DNA at positioned nucleosomes3,4. Here we present the cryo-electron microscopy structure of a ternary complex of catalytically competent DNMT3A2, the catalytically inactive accessory subunit DNMT3B3 and a nucleosome core particle flanked by linker DNA. The catalytic-like domain of the accessory DNMT3B3 binds to the acidic patch of the nucleosome core, which orients the binding of DNMT3A2 to the linker DNA. The steric constraints of this arrangement suggest that nucleosomal DNA must be moved relative to the nucleosome core for de novo methylation to occur.
DOI: 10.1038/s41586-020-2747-1
Source: https://www.nature.com/articles/s41586-020-2747-1
Nature:《自然》,创刊于1869年。隶属于施普林格·自然出版集团,最新IF:69.504
官方网址:http://www.nature.com/
投稿链接:http://www.nature.com/authors/submit_manuscript.html
本期文章:《自然》:Online/在线发表