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- W3153770199 abstract "Abstract The eukaryotic replisome is comprised of three family-B DNA polymerases (Polα, δ and ϵ). Polα forms a stable complex with primase to synthesize short RNA-DNA primers, which are subsequently elongated by Polδ and Polϵ in concert with proliferating cell nuclear antigen (PCNA). In some species of archaea, family-D DNA polymerase (PolD) is the only DNA polymerase essential for cell viability, raising the question of how it alone conducts the bulk of DNA synthesis. We used a hyperthermophilic archaeon, Thermococcus kodakarensis, to demonstrate that PolD connects primase to the archaeal replisome before interacting with PCNA. Whereas PolD stably connects primase to GINS, a component of CMG helicase, cryo-EM analysis indicated a highly flexible PolD–primase complex. A conserved hydrophobic motif at the C-terminus of the DP2 subunit of PolD, a PIP (PCNA-Interacting Peptide) motif, was critical for the interaction with primase. The dissociation of primase was induced by DNA-dependent binding of PCNA to PolD. Point mutations in the alternative PIP-motif of DP2 abrogated the molecular switching that converts the archaeal replicase from de novo to processive synthesis mode." @default.
- W3153770199 created "2021-04-26" @default.
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- W3153770199 date "2021-04-13" @default.
- W3153770199 modified "2023-10-15" @default.
- W3153770199 title "DNA polymerase D temporarily connects primase to the CMG-like helicase before interacting with proliferating cell nuclear antigen" @default.
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- W3153770199 doi "https://doi.org/10.1093/nar/gkab243" @default.
- W3153770199 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8096248" @default.
- W3153770199 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33849056" @default.
- W3153770199 hasPublicationYear "2021" @default.
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