Ubiquitylation of nucleic acids by DELTEX ubiquitin E3 ligase DTX3L

The recent discovery of non-proteinaceous ubiquitylation substrates broadened our understanding of this modification beyond conventional protein targets. However, the existence of additional types of substrates remains elusive. Here, we present evidence that nucleic acids can also be directly ubiquitylated via ester bond formation. DTX3L, a member of the DELTEX family E3 ubiquitin ligases, ubiquitylates DNA and RNA in vitro and that this activity is shared with DTX3, but not with the other DELTEX family members DTX1, DTX2 and DTX4. DTX3L shows preference for the 3'-terminal adenosine over other nucleotides. In addition, we demonstrate that ubiquitylation of nucleic acids is reversible by DUBs such as USP2, JOSD1 and SARS-CoV-2 PLpro. Overall, our study proposes reversible ubiquitylation of nucleic acids in vitro and discusses its potential functional implications.

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Publication Details

Journal
EMBO Reports
Published
2024-09-06
DOI
https://doi.org/10.1038/s44319-024-00235-1
Citations
21
Primary Topic
Ubiquitin and proteasome pathways
Type
article
Field-Weighted Citation Impact
4.91

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article

Ubiquitylation of nucleic acids by DELTEX ubiquitin E3 ligase DTX3L

Vincent Aucagne, Benedikt Mathias Kessler, Benjamin M. Foster, Ivan Ahel et al.
21 citations
EMBO Reports
Ubiquitin and proteasome pathways
4.91
article

Ubiquitylation of nucleic acids by DELTEX ubiquitin E3 ligase DTX3L

Vincent Aucagne, Benedikt Mathias Kessler, Benjamin M. Foster, Ivan Ahel, Dragana Ahel, Ian Gibbs‐Seymour, Marcin J. Suskiewicz, Kang Zhu, Chatrin Chatrin
article en
21 citations

Abstract

The recent discovery of non-proteinaceous ubiquitylation substrates broadened our understanding of this modification beyond conventional protein targets. However, the existence of additional types of substrates remains elusive. Here, we present evidence that nucleic acids can also be directly ubiquitylated via ester bond formation. DTX3L, a member of the DELTEX family E3 ubiquitin ligases, ubiquitylates DNA and RNA in vitro and that this activity is shared with DTX3, but not with the other DELTEX family members DTX1, DTX2 and DTX4. DTX3L shows preference for the 3'-terminal adenosine over other nucleotides. In addition, we demonstrate that ubiquitylation of nucleic acids is reversible by DUBs such as USP2, JOSD1 and SARS-CoV-2 PLpro. Overall, our study proposes reversible ubiquitylation of nucleic acids in vitro and discusses its potential functional implications.

EMBO ReportsVol. 25(10)
Centre National de la Recherche Scientifique (FR), University of Oxford (GB), Centre de Biophysique Moléculaire (FR), East China Normal University (CN)
Wellcome Trust, Ovarian Cancer Research Alliance, Cancer Research UK, University of Oxford, Ligue Contre le Cancer, Studium Loire Valley-Institute for Advanced Studies, Directorate for Biological Sciences, Biotechnology and Biological Sciences Research Council, European Research Council
Openalex Percentile: Top 4%
Ubiquitin and proteasome pathways
4.91
DOIOpen Access PDFOpenAlex
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