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

Francesca Mattiroli, Michael Uckelmann, Danny D. Sahtoe, Willem J. van Dijk and Titia K. Sixma ()
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Francesca Mattiroli: Netherlands Cancer Institute
Michael Uckelmann: Netherlands Cancer Institute
Danny D. Sahtoe: Netherlands Cancer Institute
Willem J. van Dijk: Netherlands Cancer Institute
Titia K. Sixma: Netherlands Cancer Institute

Nature Communications, 2014, vol. 5, issue 1, 1-11

Abstract: 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.

Date: 2014
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4291

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DOI: 10.1038/ncomms4291

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