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Functional crosstalk between histone H2B ubiquitylation and H2A modifications and variants

Author

Listed:
  • Felix Wojcik

    (Princeton University)

  • Geoffrey P. Dann

    (Princeton University
    University of Pennsylvania)

  • Leslie Y. Beh

    (Princeton University
    Princeton University
    Columbia University)

  • Galia T. Debelouchina

    (Princeton University
    University of California San Diego)

  • Raphael Hofmann

    (Princeton University
    Laboratorium für Organische Chemie)

  • Tom W. Muir

    (Princeton University)

Abstract

Ubiquitylation of histone H2B at lysine residue 120 (H2BK120ub) is a prominent histone posttranslational modification (PTM) associated with the actively transcribed genome. Although H2BK120ub triggers several critical downstream histone modification pathways and changes in chromatin structure, less is known about the regulation of the ubiquitylation reaction itself, in particular with respect to the modification status of the chromatin substrate. Here we employ an unbiased library screening approach to profile the impact of pre-existing chromatin modifications on de novo ubiquitylation of H2BK120 by the cognate human E2:E3 ligase pair, UBE2A:RNF20/40. Deposition of H2BK120ub is found to be highly sensitive to PTMs on the N-terminal tail of histone H2A, a crosstalk that extends to the common histone variant H2A.Z. Based on a series of biochemical and cell-based studies, we propose that this crosstalk contributes to the spatial organization of H2BK120ub on gene bodies, and is thus important for transcriptional regulation.

Suggested Citation

  • Felix Wojcik & Geoffrey P. Dann & Leslie Y. Beh & Galia T. Debelouchina & Raphael Hofmann & Tom W. Muir, 2018. "Functional crosstalk between histone H2B ubiquitylation and H2A modifications and variants," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03895-5
    DOI: 10.1038/s41467-018-03895-5
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    Cited by:

    1. Shuhei Onishi & Kotone Uchiyama & Ko Sato & Chikako Okada & Shunsuke Kobayashi & Keisuke Hamada & Tomohiro Nishizawa & Osamu Nureki & Kazuhiro Ogata & Toru Sengoku, 2024. "Structure of the human Bre1 complex bound to the nucleosome," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Kate M. MacDonald & Shirony Nicholson-Puthenveedu & Maha M. Tageldein & Sarika Khasnis & Cheryl H. Arrowsmith & Shane M. Harding, 2023. "Antecedent chromatin organization determines cGAS recruitment to ruptured micronuclei," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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