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Dynamics of nucleosome remodelling by individual ACF complexes

Author

Listed:
  • Timothy R. Blosser

    (Howard Hughes Medical Institute,
    Graduate Program in Biophysics, Harvard University, Cambridge, Massachusetts 02138, USA)

  • Janet G. Yang

    (University of California, San Francisco, California 94107, USA)

  • Michael D. Stone

    (Howard Hughes Medical Institute,
    Department of Chemistry and Chemical Biology,)

  • Geeta J. Narlikar

    (University of California, San Francisco, California 94107, USA)

  • Xiaowei Zhuang

    (Howard Hughes Medical Institute,
    Department of Chemistry and Chemical Biology,
    Harvard University, Cambridge, Massachusetts 02138, USA)

Abstract

The ATP-dependent chromatin assembly and remodelling factor (ACF) functions to generate regularly spaced nucleosomes, which are required for heritable gene silencing. The mechanism by which ACF mobilizes nucleosomes remains poorly understood. Here we report a single-molecule FRET study that monitors the remodelling of individual nucleosomes by ACF in real time, revealing previously unknown remodelling intermediates and dynamics. In the presence of ACF and ATP, the nucleosomes exhibit gradual translocation along DNA interrupted by well-defined kinetic pauses that occurred after approximately seven or three to four base pairs of translocation. The binding of ACF, translocation of DNA and exiting of translocation pauses are all ATP-dependent, revealing three distinct functional roles of ATP during remodelling. At equilibrium, a continuously bound ACF complex can move the nucleosome back-and-forth many times before dissociation, indicating that ACF is a highly processive and bidirectional nucleosome translocase.

Suggested Citation

  • Timothy R. Blosser & Janet G. Yang & Michael D. Stone & Geeta J. Narlikar & Xiaowei Zhuang, 2009. "Dynamics of nucleosome remodelling by individual ACF complexes," Nature, Nature, vol. 462(7276), pages 1022-1027, December.
    • Handle: RePEc:nat:nature:v:462:y:2009:i:7276:d:10.1038_nature08627
    DOI: 10.1038/nature08627
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    Cited by:

    1. Luka Bacic & Guillaume Gaullier & Jugal Mohapatra & Guanzhong Mao & Klaus Brackmann & Mikhail Panfilov & Glen Liszczak & Anton Sabantsev & Sebastian Deindl, 2024. "Asymmetric nucleosome PARylation at DNA breaks mediates directional nucleosome sliding by ALC1," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    2. Jiayi Fan & Andrew T. Moreno & Alexander S. Baier & Joseph J. Loparo & Craig L. Peterson, 2022. "H2A.Z deposition by SWR1C involves multiple ATP-dependent steps," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    3. Un Seng Chio & Eugene Palovcak & Anton A. A. Smith & Henriette Autzen & Elise N. Muñoz & Zanlin Yu & Feng Wang & David A. Agard & Jean-Paul Armache & Geeta J. Narlikar & Yifan Cheng, 2024. "Functionalized graphene-oxide grids enable high-resolution cryo-EM structures of the SNF2h-nucleosome complex without crosslinking," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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