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DNA Wrapping by a tetrameric bacterial histone

Nature Communications, vol. 16, pp. 11108

Abstract

Abstract Histones are conserved DNA-packaging proteins found across all domains of life. In eukaryotes, canonical histones form octamers that wrap ~147 base pairs (bp) of DNA into nucleosomes, while in archaea they form dimers that polymerize into extended hypernucleosomes. Although bacteria were long thought to lack histones, homologs have now been identified in diverse lineages. We previously characterized the histone HBb from Bdellovibrio bacteriovorus , which binds and bends DNA as a dimer. Here, we describe HLp from Leptospira perolatii and show by crystallographic and biophysical analyses that, unlike HBb, it forms stable tetramers and binds DNA nonspecifically, wrapping ~60 bp of DNA around its core. Molecular dynamics simulations, DNA-binding assays, and heterologous expression in Escherichia coli , where HLp reorganizes the nucleoid, support a role in bacterial chromatin organization. These findings expand the repertoire of bacterial histone-DNA interactions and highlight the diversity of histone-based genome organization across the tree of life.

Authors 12

  1. Max Planck Institute for Biology

    Affiliation as printed

    Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany

  2. Leiden University

    Affiliation as printed

    Leiden Institute of Chemistry, Leiden University, Leiden, The Netherlands; Centre for Microbial Cell Biology, Leiden University, Leiden, The Netherlands; Centre for Interdisciplinary Genome Research, Leiden University, Leiden, The Netherlands

    Centre for Interdisciplinary Genome Research, Leiden University, Leiden, The Netherlands

  3. Max Planck Institute for Biology

    Affiliation as printed

    Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany

  4. University of Illinois Urbana-Champaign

    Affiliation as printed

    Theoretical and Computational Biophysics Group, Beckman Institute for Advanced Science and Technology, Center of Biophysics and Quantitative Biology, University of Illinois Urbana-Champaign, Urbana, USA

    Theoretical and Computational Biophysics Group, Beckman Institute for Advanced Science and Technology, Center of Biophysics and Quantitative Biology, University of Illinois Urbana–Champaign, Urbana, USA

  5. Max Planck Institute for Biology

    Affiliation as printed

    Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany

  6. Max Planck Institute for Biology

    Affiliation as printed

    Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany

  7. Max Planck Institute for Biology

    Affiliation as printed

    BioOptics Facility, Max Planck Institute for Biology Tübingen, Tübingen, Germany

  8. Max Planck Institute for Biology

    Affiliation as printed

    Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany

  9. Max Planck Institute for Biology · University of Tübingen

    Affiliation as printed

    Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany

    Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany

  10. Leiden University

    Affiliation as printed

    Leiden Institute of Chemistry, Leiden University, Leiden, The Netherlands; Centre for Microbial Cell Biology, Leiden University, Leiden, The Netherlands; Centre for Interdisciplinary Genome Research, Leiden University, Leiden, The Netherlands

    Centre for Interdisciplinary Genome Research, Leiden University, Leiden, The Netherlands

  11. Vikram Alva corresponding

    Max Planck Institute for Biology

    Affiliation as printed

    Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany. vikram.alva@tuebingen.mpg.de

    Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany

  12. Birte Hernandez Alvarez corresponding

    Max Planck Institute for Biology

    Affiliation as printed

    Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany. birte.hernandez@tuebingen.mpg.de

    Department of Protein Evolution, Max Planck Institute for Biology Tübingen, Tübingen, Germany

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References 76