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The structure of (CENP-A–H4)2 reveals physical features that mark centromeres

Author

Listed:
  • Nikolina Sekulic

    (University of Pennsylvania, School of Medicine)

  • Emily A. Bassett

    (University of Pennsylvania, School of Medicine
    Graduate Group in Biochemistry and Molecular Biophysics, University of Pennsylvania, School of Medicine)

  • Danielle J. Rogers

    (University of Pennsylvania, School of Medicine)

  • Ben E. Black

    (University of Pennsylvania, School of Medicine
    Graduate Group in Biochemistry and Molecular Biophysics, University of Pennsylvania, School of Medicine)

Abstract

CENP-A makes its mark on centromeres The hallmark of all eukaryotic centromeres is the presence of a histone H3 variant, CENP-A, but the nature of the epigenetic centromere mark is the subject of great debate. The crystal structure of the human CENP-A–H4 complex has now been determined. It reveals the structural basis for the rigidity that CENP-A imparts to nucleosomes, as well as several surprising global and local structural alterations that have major implications for epigenetic centromere marking. CENP-A seems to alter the chromatin into which it assembles — not by switching the handedness of DNA wrapping or disrupting the octameric histone stoichiometry, but by altering nucleosome structure.

Suggested Citation

  • Nikolina Sekulic & Emily A. Bassett & Danielle J. Rogers & Ben E. Black, 2010. "The structure of (CENP-A–H4)2 reveals physical features that mark centromeres," Nature, Nature, vol. 467(7313), pages 347-351, September.
    • Handle: RePEc:nat:nature:v:467:y:2010:i:7313:d:10.1038_nature09323
    DOI: 10.1038/nature09323
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    Cited by:

    1. Harsh Nagpal & Ahmad Ali-Ahmad & Yasuhiro Hirano & Wei Cai & Mario Halic & Tatsuo Fukagawa & Nikolina Sekulić & Beat Fierz, 2023. "CENP-A and CENP-B collaborate to create an open centromeric chromatin state," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

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