Autoinhibitory elements of the Chd1 remodeler block initiation of twist defects by destabilizing the ATPase motor on the nucleosome

• DOI: 10.1073/pnas.2014498118
• Publication Date: 2021-01-19T22:12:05Z
• Authors: Ilana M. Nodelman; Zhongtian Shen; Robert F. Levendosky; Gregory D. Bowman
• Keywords: Adenosine Triphosphatases; 0301 basic medicine; Saccharomyces cerevisiae Proteins; Hydrolysis; Saccharomyces cerevisiae; Chromatin Assembly and Disassembly; Chromosomes; Nucleosomes; DNA-Binding Proteins; Histones; 03 medical and health sciences; Adenosine Triphosphate; Protein Domains; Protein Binding

Chromatin remodelers are ATP (adenosine triphosphate)-powered motors that reposition nucleosomes throughout eukaryotic chromosomes. Remodelers possess autoinhibitory elements control the direction of nucleosome sliding, but underlying mechanisms inhibition have been unclear. Here, we show yeast Chd1 remodeler block sliding by preventing initiation twist defects. We two elements-the chromodomains and bridge-reinforce each other to when DNA-binding domain is not bound entry-side DNA. Our data support a model where bridge target nucleotide-free ADP-bound states ATPase motor, favoring partially disengaged state motor on nucleosome. By bypassing distortions nucleosomal DNA prior binding, propose uncouple binding/hydrolysis cycle from translocation around histone core.