德国马克斯普朗克生物物理化学研究所Patrick Cramer课题组取得一项新进展。他们的最新工作揭示了SWI/SNF染色质重塑复合物RSC与核小体结合后的结构。2020年3月11日,《自然》杂志在线发表了这项成果。
Title: Structure of SWI/SNF chromatin remodeller RSC bound to a nucleosome
Author: Felix R. Wagner, Christian Dienemann, Haibo Wang, Alexandra Sttzer, Dimitry Tegunov, Henning Urlaub, Patrick Cramer
Issue&Volume: 2020-03-11
Abstract: Chromatin-remodelling complexes of the SWI/SNF family function in the formation of nucleosome-depleted, transcriptionally active promoter regions (NDRs). In the yeast Saccharomyces cerevisiae, the essential SWI/SNF complex RSC contains 16 subunits, including the ATP-dependent DNA translocase Sth1. RSC removes nucleosomes from promoter regions and positions the specialized +1 and -1 nucleosomes that flank NDRs. Here we present the cryo-electron microscopy structure of RSC in complex with a nucleosome substrate. The structure reveals that RSC forms five protein modules and suggests key features of the remodelling mechanism. The body module serves as a scaffold for the four flexible modules that we call DNA-interacting, ATPase, arm and actin-related protein (ARP) modules. The DNA-interacting module binds extra-nucleosomal DNA and is involved in the recognition of promoter DNA elements that influence RSC functionality. The ATPase and arm modules sandwich the nucleosome disc with the Snf2 ATP-coupling (SnAC) domain and the finger helix, respectively. The translocase motor of the ATPase module engages with the edge of the nucleosome at superhelical location +2. The mobile ARP module may modulate translocase–nucleosome interactions to regulate RSC activity. The RSC–nucleosome structure provides a basis for understanding NDR formation and the structure and function of human SWI/SNF complexes that are frequently mutated in cancer.
DOI: 10.1038/s41586-020-2088-0
Source: https://www.nature.com/articles/s41586-020-2088-0
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