CHD4 slides nucleosomes by decoupling entry- and exit-side DNA translocation

Yichen Zhong, Bishnu P. Paudel, Daniel P. Ryan, Jason K. K. Low, Charlotte Franck, Karishma Patel, Max J. Bedward, Mario Torrado, Richard J. Payne, Antoine M. Oijen () and Joel P. Mackay ()
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Yichen Zhong: University of Sydney
Bishnu P. Paudel: University of Wollongong
Daniel P. Ryan: The Australian National University
Jason K. K. Low: University of Sydney
Charlotte Franck: University of Sydney
Karishma Patel: University of Sydney
Max J. Bedward: University of Sydney
Mario Torrado: University of Sydney
Richard J. Payne: The University of Sydney
Antoine M. Oijen: University of Wollongong
Joel P. Mackay: University of Sydney

Nature Communications, 2020, vol. 11, issue 1, 1-14

Abstract: Abstract Chromatin remodellers hydrolyse ATP to move nucleosomal DNA against histone octamers. The mechanism, however, is only partially resolved, and it is unclear if it is conserved among the four remodeller families. Here we use single-molecule assays to examine the mechanism of action of CHD4, which is part of the least well understood family. We demonstrate that the binding energy for CHD4-nucleosome complex formation—even in the absence of nucleotide—triggers significant conformational changes in DNA at the entry side, effectively priming the system for remodelling. During remodelling, flanking DNA enters the nucleosome in a continuous, gradual manner but exits in concerted 4–6 base-pair steps. This decoupling of entry- and exit-side translocation suggests that ATP-driven movement of entry-side DNA builds up strain inside the nucleosome that is subsequently released at the exit side by DNA expulsion. Based on our work and previous studies, we propose a mechanism for nucleosome sliding.

Date: 2020
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DOI: 10.1038/s41467-020-15183-2

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