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Plasmodium belongs to the phylum Apicomplexa and, like most members of this phylum, contains a non-photosynthetic plastid called the apicoplast.\u00a0The apicoplast has its own genome, replicated by a dedicated replisome. Unlike other cellular replisomes, the apicoplast replisome uses a single DNA polymerase (apPol). This suggests that apPol can multitask and catalyse both replicative and lesion bypass synthesis. Replicative synthesis relies on a restrictive active site for high accuracy while lesion bypass typically\u00a0requires an open active site. This raises the question: how does apPol combine the structural features of multiple DNA polymerases in a single protein? Using single-particle electron cryomicroscopy (cryoEM), we have solved the structures of apPol bound to its undamaged DNA and nucleotide substrates in five pre-chemistry conformational states. We found that apPol can accommodate a nascent base pair with the fingers in an open configuration, which might facilitate the lesion bypass activity. In the fingers-open state, we identified a nascent base pair checkpoint that preferentially selects Watson\u2013Crick base pairs, an essential requirement for replicative synthesis. Taken together, these structural features might explain how apPol balances replicative and lesion bypass synthesis.<\/jats:p>","DOI":"10.1093\/nar\/gkaf1005","type":"journal-article","created":{"date-parts":[[2025,10,16]],"date-time":"2025-10-16T13:27:55Z","timestamp":1760621275000},"source":"Crossref","is-referenced-by-count":0,"title":["Structural basis of multitasking by the apicoplast DNA polymerase from <i>Plasmodium falciparum<\/i>"],"prefix":"10.1093","volume":"53","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8431-0951","authenticated-orcid":false,"given":"Anamika","family":"Kumari","sequence":"first","affiliation":[{"name":"Molecular Microbiology, School of Biosciences, The University of Sheffield , Sheffield\u00a0 S10 2TN 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