Structural highlights
Publication Abstract from PubMed
Replicative DNA polymerases duplicate entire genomes at high fidelity. This feature is shared among the three domains of life and is facilitated by their dual polymerase and exonuclease activities. Family D replicative DNA polymerases (PolD), found exclusively in Archaea, contain an unusual RNA polymerase-like catalytic core, and a unique Mre11-like proofreading active site. Here, we present cryo-EM structures of PolD trapped in a proofreading mode, revealing an unanticipated correction mechanism that extends the repertoire of protein domains known to be involved in DNA proofreading. Based on our experimental structures, mutants of PolD were designed and their contribution to mismatch bypass and exonuclease kinetics was determined. This study sheds light on the convergent evolution of structurally distinct families of DNA polymerases, and the domain acquisition and exchange mechanism that occurred during the evolution of the replisome in the three domains of life.
Molecular basis for proofreading by the unique exonuclease domain of Family-D DNA polymerases.,Betancurt-Anzola L, Martinez-Carranza M, Delarue M, Zatopek KM, Gardner AF, Sauguet L Nat Commun. 2023 Dec 14;14(1):8306. doi: 10.1038/s41467-023-44125-x. PMID:38097591[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Betancurt-Anzola L, Martínez-Carranza M, Delarue M, Zatopek KM, Gardner AF, Sauguet L. Molecular basis for proofreading by the unique exonuclease domain of Family-D DNA polymerases. Nat Commun. 2023 Dec 14;14(1):8306. PMID:38097591 doi:10.1038/s41467-023-44125-x
