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Remodelers tap into nucleosome plasticity

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Chromatin-remodeling enzymes perform the formidable task of reorganizing the structure of a stable macromolecular assembly, the nucleosome. Recently published work demonstrates that the SNF2H chromatin remodeler distorts the histone octamer structure upon binding to the nucleosome, then taps into this induced plasticity to productively achieve nucleosome sliding.

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Figure 1: A model for the role of histone octamer distortion in nucleosome sliding.

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Acknowledgements

We acknowledge support from the Deutsche Forschungsgemeinschaft (SFB 646 and 1064 to A.G.L.; SFB 1064 to H.R.S.) and from the European Commission (Marie Skłodowska Curie Individual Fellowship 'SilentFACT' and H2020-MSCA-IF-2014 contract 657244 to M.M.).

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Authors and Affiliations

  1. Hari R. Singh and Magdalena Murawska are at the Department of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, Planegg-Martinsried, Germany.,

    Hari R Singh & Magdalena Murawska

  2. Andreas G. Ladurner is at the Department of Physiological Chemistry, Biomedical Center, Ludwig-Maximilians-University of Munich, Planegg-Martinsried, Germany; the International Max Planck Research School for Molecular and Cellular Life Sciences, Martinsried, Germany; the Center for Integrated Protein Science Munich (CIPSM), Munich, Germany; and the Munich Cluster for Systems Neurology (SyNergy), Munich, Germany,

    Andreas G Ladurner

  3. the International Max Planck Research School for Molecular and Cellular Life Sciences, Martinsried, Germany,

    Andreas G Ladurner

Authors
  1. Hari R Singh
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  2. Magdalena Murawska
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  3. Andreas G Ladurner
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Correspondence to Andreas G Ladurner.

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Competing interests

A.G.L. is on the Scientific Advisory Board of VolitionRx, Inc.

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Singh, H., Murawska, M. & Ladurner, A. Remodelers tap into nucleosome plasticity. Nat Struct Mol Biol 24, 341–343 (2017). https://doi.org/10.1038/nsmb.3394

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