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

Journal Article


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Abstract


  • © 2020, The Author(s). 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.

Authors


  •   Zhong, Yichen (external author)
  •   Paudel, Bishnu
  •   Ryan, Daniel (external author)
  •   Low, Jason (external author)
  •   Franck, Charlotte (external author)
  •   Patel, Karishma (external author)
  •   Bedward, Max (external author)
  •   Torrado, Mario (external author)
  •   Payne, Richard (external author)
  •   van Oijen, Antoine M.
  •   Mackay, Joel (external author)

Publication Date


  • 2020

Citation


  • Zhong, Y., Paudel, B. P., Ryan, D. P., Low, J. K.K., Franck, C., Patel, K., Bedward, M. J., Torrado, M., Payne, R. J., van Oijen, A. M. & Mackay, J. P. (2020). CHD4 slides nucleosomes by decoupling entry- and exit-side DNA translocation. Nature Communications, 11 (1), 1-14.

Scopus Eid


  • 2-s2.0-85082508825

Ro Full-text Url


  • https://ro.uow.edu.au/cgi/viewcontent.cgi?article=2292&context=smhpapers1

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers1/1274

Has Global Citation Frequency


Number Of Pages


  • 13

Start Page


  • 1

End Page


  • 14

Volume


  • 11

Issue


  • 1

Place Of Publication


  • United Kingdom

Abstract


  • © 2020, The Author(s). 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.

Authors


  •   Zhong, Yichen (external author)
  •   Paudel, Bishnu
  •   Ryan, Daniel (external author)
  •   Low, Jason (external author)
  •   Franck, Charlotte (external author)
  •   Patel, Karishma (external author)
  •   Bedward, Max (external author)
  •   Torrado, Mario (external author)
  •   Payne, Richard (external author)
  •   van Oijen, Antoine M.
  •   Mackay, Joel (external author)

Publication Date


  • 2020

Citation


  • Zhong, Y., Paudel, B. P., Ryan, D. P., Low, J. K.K., Franck, C., Patel, K., Bedward, M. J., Torrado, M., Payne, R. J., van Oijen, A. M. & Mackay, J. P. (2020). CHD4 slides nucleosomes by decoupling entry- and exit-side DNA translocation. Nature Communications, 11 (1), 1-14.

Scopus Eid


  • 2-s2.0-85082508825

Ro Full-text Url


  • https://ro.uow.edu.au/cgi/viewcontent.cgi?article=2292&context=smhpapers1

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers1/1274

Has Global Citation Frequency


Number Of Pages


  • 13

Start Page


  • 1

End Page


  • 14

Volume


  • 11

Issue


  • 1

Place Of Publication


  • United Kingdom