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Linker histone H1 and H3K56 acetylation are antagonistic regulators of nucleosome dynamics

Author

Listed:
  • Morgan Bernier

    (The Ohio State University)

  • Yi Luo

    (Biophysics Graduate Program, The Ohio State University)

  • Kingsley C. Nwokelo

    (The Ohio State University)

  • Michelle Goodwin

    (The Ohio State University)

  • Sarah J. Dreher

    (The Ohio State Biochemistry Program, The Ohio State University)

  • Pei Zhang

    (The Ohio State University)

  • Mark R. Parthun

    (The Ohio State University)

  • Yvonne Fondufe-Mittendorf

    (University of Kentucky)

  • Jennifer J. Ottesen

    (Biophysics Graduate Program, The Ohio State University
    The Ohio State Biochemistry Program, The Ohio State University
    The Ohio State University)

  • Michael G. Poirier

    (The Ohio State University
    Biophysics Graduate Program, The Ohio State University
    The Ohio State Biochemistry Program, The Ohio State University
    The Ohio State University)

Abstract

H1 linker histones are highly abundant proteins that compact nucleosomes and chromatin to regulate DNA accessibility and transcription. However, the mechanisms that target H1 regulation to specific regions of eukaryotic genomes are unknown. Here we report fluorescence measurements of human H1 regulation of nucleosome dynamics and transcription factor (TF) binding within nucleosomes. H1 does not block TF binding, instead it suppresses nucleosome unwrapping to reduce DNA accessibility within H1-bound nucleosomes. We then investigated H1 regulation by H3K56 and H3K122 acetylation, two transcriptional activating histone post translational modifications (PTMs). Only H3K56 acetylation, which increases nucleosome unwrapping, abolishes H1.0 reduction of TF binding. These findings show that nucleosomes remain dynamic, while H1 is bound and H1 dissociation is not required for TF binding within the nucleosome. Furthermore, our H3K56 acetylation measurements suggest that a single-histone PTM can define regions of the genome that are not regulated by H1.

Suggested Citation

  • Morgan Bernier & Yi Luo & Kingsley C. Nwokelo & Michelle Goodwin & Sarah J. Dreher & Pei Zhang & Mark R. Parthun & Yvonne Fondufe-Mittendorf & Jennifer J. Ottesen & Michael G. Poirier, 2015. "Linker histone H1 and H3K56 acetylation are antagonistic regulators of nucleosome dynamics," Nature Communications, Nature, vol. 6(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms10152
    DOI: 10.1038/ncomms10152
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    Cited by:

    1. Angelina M. Georgieva & Xinyue Guo & Marek Bartkuhn & Stefan Günther & Carsten Künne & Christian Smolka & Ann Atzberger & Ulrich Gärtner & Kamel Mamchaoui & Eva Bober & Yonggang Zhou & Xuejun Yuan & T, 2022. "Inactivation of Sirt6 ameliorates muscular dystrophy in mdx mice by releasing suppression of utrophin expression," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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