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Structure and mechanism of the chromatin remodelling factor ISW1a

Author

Listed:
  • Kazuhiro Yamada

    (ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20)

  • Timothy D. Frouws

    (ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20)

  • Brigitte Angst

    (ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20)

  • Daniel J. Fitzgerald

    (ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20
    Present addresses: Blueshift Pharma, Technoparkstrasse 1, CH-8005 Zürich, Switzerland (D.J.F.); Helix BioPharma Corp., 1036 Parsons Road, Edmonton, Alberta T6X 0J4, Canada (C.D.).)

  • Carl DeLuca

    (ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20
    Present addresses: Blueshift Pharma, Technoparkstrasse 1, CH-8005 Zürich, Switzerland (D.J.F.); Helix BioPharma Corp., 1036 Parsons Road, Edmonton, Alberta T6X 0J4, Canada (C.D.).)

  • Kyoko Schimmele

    (ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20)

  • David F. Sargent

    (ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20)

  • Timothy J. Richmond

    (ETH Zürich, Institute of Molecular Biology and Biophysics, Schafmattstr. 20)

Abstract

Site-specific recognition of DNA in eukaryotic organisms depends on the arrangement of nucleosomes in chromatin. In the yeast Saccharomyces cerevisiae, ISW1a and related chromatin remodelling factors are implicated in establishing the nucleosome repeat during replication and altering nucleosome position to affect gene activity. Here we have solved the crystal structures of S. cerevisiae ISW1a lacking its ATPase domain both alone and with DNA bound at resolutions of 3.25 Å and 3.60 Å, respectively, and we have visualized two different nucleosome-containing remodelling complexes using cryo-electron microscopy. The composite X-ray and electron microscopy structures combined with site-directed photocrosslinking analyses of these complexes suggest that ISW1a uses a dinucleosome substrate for chromatin remodelling. Results from a remodelling assay corroborate the dinucleosome model. We show how a chromatin remodelling factor could set the spacing between two adjacent nucleosomes acting as a ‘protein ruler’.

Suggested Citation

  • Kazuhiro Yamada & Timothy D. Frouws & Brigitte Angst & Daniel J. Fitzgerald & Carl DeLuca & Kyoko Schimmele & David F. Sargent & Timothy J. Richmond, 2011. "Structure and mechanism of the chromatin remodelling factor ISW1a," Nature, Nature, vol. 472(7344), pages 448-453, April.
    • Handle: RePEc:nat:nature:v:472:y:2011:i:7344:d:10.1038_nature09947
    DOI: 10.1038/nature09947
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    Cited by:

    1. Ashish Kumar Singh & Tamás Schauer & Lena Pfaller & Tobias Straub & Felix Mueller-Planitz, 2021. "The biogenesis and function of nucleosome arrays," Nature Communications, Nature, vol. 12(1), pages 1-15, December.

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