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High precision FRET studies reveal reversible transitions in nucleosomes between microseconds and minutes

Author

Listed:
  • Alexander Gansen

    (DKFZ, Div. Biophysics of Macromolecules)

  • Suren Felekyan

    (Lehrstuhl für Molekulare Physikalische Chemie)

  • Ralf Kühnemuth

    (Lehrstuhl für Molekulare Physikalische Chemie)

  • Kathrin Lehmann

    (DKFZ, Div. Biophysics of Macromolecules
    Lehrstuhl für Molekulare Physikalische Chemie)

  • Katalin Tóth

    (DKFZ, Div. Biophysics of Macromolecules)

  • Claus A. M. Seidel

    (Lehrstuhl für Molekulare Physikalische Chemie)

  • Jörg Langowski

    (DKFZ, Div. Biophysics of Macromolecules)

Abstract

Nucleosomes play a dual role in compacting the genome and regulating the access to DNA. To unravel the underlying mechanism, we study fluorescently labeled mononucleosomes by multi-parameter FRET measurements and characterize their structural and dynamic heterogeneity upon NaCl-induced destabilization. Species-selective fluorescence lifetime analysis and dynamic photon distribution analysis reveal intermediates during nucleosome opening and lead to a coherent structural and kinetic model. In dynamic octasomes and hexasomes the interface between the H2A-H2B dimers and the (H3-H4)2 tetramer opens asymmetrically by an angle of ≈20° on a 50 and 15 µs time scale, respectively. This is followed by a slower stepwise release of the dimers coupled with DNA unwrapping. A mutation (H2A-R81A) at the interface between H2A and H3 facilitates initial opening, confirming the central role of the dimer:tetramer interface for nucleosome stability. Partially opened states such as those described here might serve as convenient nucleation sites for DNA-recognizing proteins.

Suggested Citation

  • Alexander Gansen & Suren Felekyan & Ralf Kühnemuth & Kathrin Lehmann & Katalin Tóth & Claus A. M. Seidel & Jörg Langowski, 2018. "High precision FRET studies reveal reversible transitions in nucleosomes between microseconds and minutes," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06758-1
    DOI: 10.1038/s41467-018-06758-1
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    Cited by:

    1. László Imre & Péter Nánási & Ibtissem Benhamza & Kata Nóra Enyedi & Gábor Mocsár & Rosevalentine Bosire & Éva Hegedüs & Erfaneh Firouzi Niaki & Ágota Csóti & Zsuzsanna Darula & Éva Csősz & Szilárd Pól, 2024. "Epigenetic modulation via the C-terminal tail of H2A.Z," Nature Communications, Nature, vol. 15(1), pages 1-21, December.

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