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Nucleosome-Chd1 structure and implications for chromatin remodelling.

Lucas Farnung1, Seychelle M Vos1, Christoph Wigge1

  • 1Max Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Am Fassberg 11, 37077 Göttingen, Germany.

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Chromodomain-helicase-DNA binding protein 1 (Chd1) remodels nucleosomes by detaching DNA and positioning its ATPase motor for translocation. This structural insight reveals how Chd1 facilitates DNA transcription and maintains cellular pluripotency.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Epigenetics

Background:

  • Chromatin remodeling factors are crucial for DNA processes like transcription, replication, and repair.
  • The conserved chromodomain-helicase-DNA binding protein 1 (Chd1) plays roles in nucleosome spacing, RNA polymerase II passage, and cellular pluripotency.

Purpose of the Study:

  • To determine the cryo-electron microscopy structure of yeast Saccharomyces cerevisiae Chd1 bound to a nucleosome.
  • To elucidate the mechanism by which Chd1 remodels nucleosomes and influences DNA accessibility.

Main Methods:

  • Cryo-electron microscopy at 4.8 Å resolution.
  • Structural analysis of Chd1-nucleosome complex.

Main Results:

  • Chd1 detaches two DNA turns from the histone octamer, binding between DNA gyres in a catalytically poised state.
  • Specific domains (SANT, SLIDE, ATPase motor) interact with DNA at defined superhelical locations (SHL) and histone H4.
  • The double chromodomain facilitates ATPase closure, enabling DNA translocation and nucleosome remodeling.

Conclusions:

  • The structure reveals Chd1's mechanism for loosening DNA gyres and remodeling nucleosomes.
  • Chd1's ATPase activity, potentially involving a ratcheting mechanism, is key to its function in chromatin regulation.
  • This provides a structural basis for Chd1's role in transcription and pluripotency.