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Using a combination of yeast two-hybrid screening, mycobacterial protein fragment complementation, and biochemical analyses with purified proteins, we show that dUTPase physically interacts with the N-terminal region of AdnA and modulates the activity of the AdnAB helicase\u2013nuclease complex. Biochemical assays demonstrate that Dut enhances AdnAB activity on DNA substrates and alters the AdnAB\u2013DNA interaction. Mutational perturbation of Dut, including catalytic inactivation or deletion of a mycobacteria-specific surface loop, reduces its stimulatory effect on AdnAB in vitro and decreases recombination efficiency in mycobacterial cells. Together, these results support a functional connection between dUTPase and the AdnAB DNA-processing machinery and suggest a potential link between nucleotide metabolism and DNA repair pathways.<\/jats:p>","DOI":"10.1093\/nar\/gkag660","type":"journal-article","created":{"date-parts":[[2026,6,18]],"date-time":"2026-06-18T11:41:12Z","timestamp":1781782872000},"source":"Crossref","is-referenced-by-count":0,"title":["dUTPase modulates mycobacterial homologous recombination and interacts with the AdnAB helicase\u2013nuclease"],"prefix":"10.1093","volume":"54","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0393-3290","authenticated-orcid":false,"given":"Rita","family":"Hirmond\u00f3","sequence":"first","affiliation":[{"name":"Institute of Molecular Life Sciences, HUN-REN Research Centre for Natural Sciences , Budapest 1117 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