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The nucleosome acidic patch plays a critical role in RNF168-dependent ubiquitination of histone H2A

Author

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  • Francesca Mattiroli

    (Netherlands Cancer Institute
    Present address: Howard Hughes Medical Institute and Department of Molecular and Radiological Biosciences, Colorado State University, 1870 Campus Delivery, Fort Collins, Colorado 80523, USA)

  • Michael Uckelmann

    (Netherlands Cancer Institute)

  • Danny D. Sahtoe

    (Netherlands Cancer Institute)

  • Willem J. van Dijk

    (Netherlands Cancer Institute)

  • Titia K. Sixma

    (Netherlands Cancer Institute)

Abstract

During DNA damage response, the RING E3 ligase RNF168 ubiquitinates nucleosomal H2A at K13–15. Here we show that the ubiquitination reaction is regulated by its substrate. We define a region on the RING domain important for target recognition and identify the H2A/H2B dimer as the minimal substrate to confer lysine specificity to the RNF168 reaction. Importantly, we find an active role for the substrate in the reaction. H2A/H2B dimers and nucleosomes enhance the E3-mediated discharge of ubiquitin from the E2 and redirect the reaction towards the relevant target, in a process that depends on an intact acidic patch. This active contribution of a region distal from the target lysine provides regulation of the specific K13–15 ubiquitination reaction during the complex signalling process at DNA damage sites.

Suggested Citation

  • Francesca Mattiroli & Michael Uckelmann & Danny D. Sahtoe & Willem J. van Dijk & Titia K. Sixma, 2014. "The nucleosome acidic patch plays a critical role in RNF168-dependent ubiquitination of histone H2A," Nature Communications, Nature, vol. 5(1), pages 1-11, May.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4291
    DOI: 10.1038/ncomms4291
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