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Columnar structure of human telomeric chromatin

Author

Listed:
  • Aghil Soman

    (Nanyang Technological University)

  • Sook Yi Wong

    (Nanyang Technological University
    Duke-NUS, Medical School)

  • Nikolay Korolev

    (Nanyang Technological University)

  • Wahyu Surya

    (Nanyang Technological University)

  • Simon Lattmann

    (Nanyang Technological University
    Nanyang Technological University)

  • Vinod K. Vogirala

    (Nanyang Technological University
    Harwell Science and Innovation Campus)

  • Qinming Chen

    (Nanyang Technological University)

  • Nikolay V. Berezhnoy

    (Nanyang Technological University
    Nanyang Technological University)

  • John Noort

    (Nanyang Technological University
    Leiden University)

  • Daniela Rhodes

    (Nanyang Technological University
    Nanyang Technological University
    Laboratory of Molecular Biology)

  • Lars Nordenskiöld

    (Nanyang Technological University
    Nanyang Technological University)

Abstract

Telomeres, the ends of eukaryotic chromosomes, play pivotal parts in ageing and cancer and are targets of DNA damage and the DNA damage response1–5. Little is known about the structure of telomeric chromatin at the molecular level. Here we used negative stain electron microscopy and single-molecule magnetic tweezers to characterize 3-kbp-long telomeric chromatin fibres. We also obtained the cryogenic electron microscopy structure of the condensed telomeric tetranucleosome and its dinucleosome unit. The structure displayed close stacking of nucleosomes with a columnar arrangement, and an unusually short nucleosome repeat length that comprised about 132 bp DNA wound in a continuous superhelix around histone octamers. This columnar structure is primarily stabilized by the H2A carboxy-terminal and histone amino-terminal tails in a synergistic manner. The columnar conformation results in exposure of the DNA helix, which may make it susceptible to both DNA damage and the DNA damage response. The conformation also exists in an alternative open state, in which one nucleosome is unstacked and flipped out, which exposes the acidic patch of the histone surface. The structural features revealed in this work suggest mechanisms by which protein factors involved in telomere maintenance can access telomeric chromatin in its compact form.

Suggested Citation

  • Aghil Soman & Sook Yi Wong & Nikolay Korolev & Wahyu Surya & Simon Lattmann & Vinod K. Vogirala & Qinming Chen & Nikolay V. Berezhnoy & John Noort & Daniela Rhodes & Lars Nordenskiöld, 2022. "Columnar structure of human telomeric chromatin," Nature, Nature, vol. 609(7929), pages 1048-1055, September.
  • Handle: RePEc:nat:nature:v:609:y:2022:i:7929:d:10.1038_s41586-022-05236-5
    DOI: 10.1038/s41586-022-05236-5
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    Cited by:

    1. Joana Segura & Ofelia Díaz-Ingelmo & Belén Martínez-García & Alba Ayats-Fraile & Christoforos Nikolaou & Joaquim Roca, 2024. "Nucleosomal DNA has topological memory," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

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