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♦ See referenced article, J. Biol. Chem. 2010, 285, 27664–27672
Herpes simplex virus-1 (HSV-1) is a large double-stranded DNA virus that encodes its own suite of machinery to carry out replication and other DNA transactions. Among these are a uracil DNA glycosylase, encoded by UL2, and a dUTPase, encoded by UL50, which reduce the pool of dUTP to prevent uracil misincorporation by the viral polymerase. In this Paper of the Week, Federica Bogani and colleagues now show, both in recombinant and natural infected cell settings, that the UL2 associates with the viral replisome through an interaction with UL30, the catalytic subunit of the HSV-1 DNA polymerase. In addition, they found that UL2 co-localizes with UL30 to nuclear viral prereplicative sites, and through primer extension studies they discovered that this interaction results in the stalling of DNA synthesis at template uracils due to their conversion into non-instructional abasic sites. These findings support the existence of a viral repair complex that may be capable of replication-coupled base excision repair, revealing another mechanism by which viruses ensure genome maintenance during their critical replication cycles.