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Histones and histone variant families in prokaryotes

Author

Listed:
  • Samuel Schwab

    (Leiden University
    Leiden University
    Leiden University)

  • Yimin Hu

    (Max Planck Institute for Biology Tübingen)

  • Bert Erp

    (Leiden University
    Leiden University
    Leiden University)

  • Marc K. M. Cajili

    (Leiden University
    Leiden University
    Leiden University)

  • Marcus D. Hartmann

    (Max Planck Institute for Biology Tübingen
    University of Tübingen)

  • Birte Hernandez Alvarez

    (Max Planck Institute for Biology Tübingen)

  • Vikram Alva

    (Max Planck Institute for Biology Tübingen)

  • Aimee L. Boyle

    (Leiden University
    Leiden University
    Leiden University
    University of Bristol)

  • Remus T. Dame

    (Leiden University
    Leiden University
    Leiden University)

Abstract

Histones are important chromatin-organizing proteins in eukaryotes and archaea. They form superhelical structures around which DNA is wrapped. Recent studies have shown that some archaea and bacteria contain alternative histones that exhibit different DNA binding properties, in addition to highly divergent sequences. However, the vast majority of these histones are identified in metagenomes and thus are difficult to study in vivo. The recent revolutionary breakthroughs in computational protein structure prediction by AlphaFold2 and RoseTTAfold allow for unprecedented insights into the potential function and structure of previously uncharacterized proteins. Here, we categorize the prokaryotic histone space into 17 distinct groups based on AlphaFold2 predictions. We identify a superfamily of histones, termed α3 histones, which are common in archaea and present in several bacteria. Importantly, we establish the existence of a large family of histones throughout archaea and in some bacteriophages that, instead of wrapping DNA, bridge DNA, thereby diverging from conventional nucleosomal histones.

Suggested Citation

  • Samuel Schwab & Yimin Hu & Bert Erp & Marc K. M. Cajili & Marcus D. Hartmann & Birte Hernandez Alvarez & Vikram Alva & Aimee L. Boyle & Remus T. Dame, 2024. "Histones and histone variant families in prokaryotes," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-52337-y
    DOI: 10.1038/s41467-024-52337-y
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    References listed on IDEAS

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    1. John Jumper & Richard Evans & Alexander Pritzel & Tim Green & Michael Figurnov & Olaf Ronneberger & Kathryn Tunyasuvunakool & Russ Bates & Augustin Žídek & Anna Potapenko & Alex Bridgland & Clemens Me, 2021. "Highly accurate protein structure prediction with AlphaFold," Nature, Nature, vol. 596(7873), pages 583-589, August.
    2. Karolin Luger & Armin W. Mäder & Robin K. Richmond & David F. Sargent & Timothy J. Richmond, 1997. "Crystal structure of the nucleosome core particle at 2.8 Å resolution," Nature, Nature, vol. 389(6648), pages 251-260, September.
    3. Robert C. Edgar, 2022. "Muscle5: High-accuracy alignment ensembles enable unbiased assessments of sequence homology and phylogeny," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
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