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Site-specific ubiquitylation acts as a regulator of linker histone H1

Author

Listed:
  • Eva Höllmüller

    (University of Konstanz
    University of Konstanz
    University of Konstanz)

  • Simon Geigges

    (University of Konstanz
    University of Konstanz)

  • Marie L. Niedermeier

    (University of Konstanz
    University of Konstanz)

  • Kai-Michael Kammer

    (University of Konstanz
    University of Konstanz)

  • Simon M. Kienle

    (University of Konstanz
    University of Konstanz)

  • Daniel Rösner

    (University of Konstanz
    University of Konstanz)

  • Martin Scheffner

    (University of Konstanz
    University of Konstanz)

  • Andreas Marx

    (University of Konstanz
    University of Konstanz)

  • Florian Stengel

    (University of Konstanz
    University of Konstanz)

Abstract

Decoding the role of histone posttranslational modifications (PTMs) is key to understand the fundamental process of epigenetic regulation. This is well studied for PTMs of core histones but not for linker histone H1 in general and its ubiquitylation in particular due to a lack of proper tools. Here, we report on the chemical synthesis of site-specifically mono-ubiquitylated H1.2 and identify its ubiquitin-dependent interactome on a proteome-wide scale. We show that site-specific ubiquitylation of H1 at position K64 modulates interactions with deubiquitylating enzymes and the deacetylase SIRT1. Moreover, it affects H1-dependent chromatosome assembly and phase separation resulting in a more open chromatosome conformation generally associated with a transcriptionally active chromatin state. In summary, we propose that site-specific ubiquitylation plays a general regulatory role for linker histone H1.

Suggested Citation

  • Eva Höllmüller & Simon Geigges & Marie L. Niedermeier & Kai-Michael Kammer & Simon M. Kienle & Daniel Rösner & Martin Scheffner & Andreas Marx & Florian Stengel, 2021. "Site-specific ubiquitylation acts as a regulator of linker histone H1," Nature Communications, Nature, vol. 12(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23636-5
    DOI: 10.1038/s41467-021-23636-5
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