Columnar structure of human telomeric chromatin

Aghil Soman, Sook Yi Wong, Nikolay Korolev, Wahyu Surya, Simon Lattmann, Vinod K. Vogirala, Qinming Chen, Nikolay V. Berezhnoy, John Noort, Daniela Rhodes () and Lars Nordenskiöld ()
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Aghil Soman: Nanyang Technological University
Sook Yi Wong: Nanyang Technological University
Nikolay Korolev: Nanyang Technological University
Wahyu Surya: Nanyang Technological University
Simon Lattmann: Nanyang Technological University
Vinod K. Vogirala: Nanyang Technological University
Qinming Chen: Nanyang Technological University
Nikolay V. Berezhnoy: Nanyang Technological University
John Noort: Nanyang Technological University
Daniela Rhodes: Nanyang Technological University
Lars Nordenskiöld: Nanyang Technological University

Nature, 2022, vol. 609, issue 7929, 1048-1055

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41586-022-05236-5

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