Autoinhibitory elements of the Chd1 remodeler block initiation of twist defects by destabilizing the ATPase motor on the nucleosome
| Autor: | Robert F Levendosky, Gregory D. Bowman, Ilana M. Nodelman, Zhongtian Shen |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Saccharomyces cerevisiae Proteins
ATPase Allosteric regulation Saccharomyces cerevisiae Chromosomes Chromatin remodeling Histones chemistry.chemical_compound Adenosine Triphosphate Protein Domains Nucleosome Adenosine Triphosphatases Multidisciplinary biology Chemistry Hydrolysis Biological Sciences Chromatin Assembly and Disassembly Nucleosomes Chromatin DNA-Binding Proteins Histone Biophysics biology.protein Adenosine triphosphate DNA Protein Binding |
| Zdroj: | Proc Natl Acad Sci U S A |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.2014498118 |
| Popis: | Chromatin remodelers are ATP (adenosine triphosphate)-powered motors that reposition nucleosomes throughout eukaryotic chromosomes. Remodelers possess autoinhibitory elements that control the direction of nucleosome sliding, but underlying mechanisms of inhibition have been unclear. Here, we show that autoinhibitory elements of the yeast Chd1 remodeler block nucleosome sliding by preventing initiation of twist defects. We show that two autoinhibitory elements—the chromodomains and bridge—reinforce each other to block sliding when the DNA-binding domain is not bound to entry-side DNA. Our data support a model where the chromodomains and bridge target nucleotide-free and ADP-bound states of the ATPase motor, favoring a partially disengaged state of the ATPase motor on the nucleosome. By bypassing distortions of nucleosomal DNA prior to ATP binding, we propose that autoinhibitory elements uncouple the ATP binding/hydrolysis cycle from DNA translocation around the histone core. |
| Databáze: | OpenAIRE |
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