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Historically defined as a protein post-translational modification, ADP-ribosylation on nucleic acids has been increasingly recognized in recent years, particularly in bacterial systems, but remains poorly understood in higher organisms. Here, we identify human PARP10 as a candidate enzyme that ADP-ribosylates nucleic acid bases, showing apparent activity on uracil bases in RNA, and a relatively weaker activity toward thymine bases in DNA. Furthermore, we show that human TARG1, a neurodegenerative disorder-linked protein previously reported to hydrolyse thymine base ADP-ribosylation, also efficiently reverses uracil base ADP-ribosylation (U-ADPr). To improve the efficient characterization of the enzymes for U-ADPr reversal, we developed chemical probes. Using these probes, we demonstrated that human TARG1 and TARG1-like macrodomain proteins are the efficient hydrolases for U-ADPr reversal in humans,\u00a0Drosophila melanogaster, and bacterial homologues. The widespread distribution of U-ADPr hydrolases among different organisms suggests the potential evolutionary conservation of U-ADPr as a biological signal.<\/jats:p>","DOI":"10.1093\/nar\/gkag289","type":"journal-article","created":{"date-parts":[[2026,3,18]],"date-time":"2026-03-18T13:00:05Z","timestamp":1773838805000},"source":"Crossref","is-referenced-by-count":3,"title":["Reversible RNA ADP-ribosylation on uracil bases"],"prefix":"10.1093","volume":"54","author":[{"given":"Yang","family":"Lu","sequence":"first","affiliation":[{"name":"Sir William Dunn School of Pathology, University of Oxford , OxfordOX1 3RE ,","place":["United Kingdom"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Li","family":"Tang","sequence":"additional","affiliation":[{"name":"Carbohydrate-Based Drug Research Centre, Shanghai Institute of Materia Medica, Chinese Academy of Sciences , Shanghai 201203 ,","place":["China"]},{"name":"Zhongshan Institute for Drug Discovery, Chinese Academy of 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