Stepwise nucleosome translocation by RSC remodeling complexes

The SWI/SNF-family remodelers regulate chromatin structure by coupling the free energy from ATP hydrolysis to the repositioning and restructuring of nucleosomes, but how the ATPase activity of these enzymes drives the motion of DNA across the nucleosome remains unclear. Here, we used single-molecule...

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Bibliographic Details
Published in:eLife 2016-02, Vol.5
Main Authors: Harada, Bryan T, Hwang, William L, Deindl, Sebastian, Chatterjee, Nilanjana, Bartholomew, Blaine, Zhuang, Xiaowei
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Biochemistry
Biophysics and Structural Biology
Chromatin
Deoxyribonucleic acid
DNA
DNA-Binding Proteins - metabolism
Fluorescence Resonance Energy Transfer
Free energy
FRET
Genetic aspects
Genetic research
Histones - analysis
Labeling
Microbial enzymes
Nucleosomes
Nucleosomes - metabolism
remodeling
RSC
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
single-molecule
SWI/SNF
Transcription Factors - metabolism
Translocation (Genetics)
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Summary:The SWI/SNF-family remodelers regulate chromatin structure by coupling the free energy from ATP hydrolysis to the repositioning and restructuring of nucleosomes, but how the ATPase activity of these enzymes drives the motion of DNA across the nucleosome remains unclear. Here, we used single-molecule FRET to monitor the remodeling of mononucleosomes by the yeast SWI/SNF remodeler, RSC. We observed that RSC primarily translocates DNA around the nucleosome without substantial displacement of the H2A-H2B dimer. At the sites where DNA enters and exits the nucleosome, the DNA moves largely along or near its canonical wrapping path. The translocation of DNA occurs in a stepwise manner, and at both sites where DNA enters and exits the nucleosome, the step size distributions exhibit a peak at approximately 1-2 bp. These results suggest that the movement of DNA across the nucleosome is likely coupled directly to DNA translocation by the ATPase at its binding site inside the nucleosome.
ISSN:2050-084X
2050-084X
DOI:10.7554/eLife.10051