Movie
Controller
Structure viewers
About Yorodumi Papers
+Search query
-Structure paper
| Title | DNA polymerase D temporarily connects primase to the CMG-like helicase before interacting with proliferating cell nuclear antigen. |
|---|---|
| Journal, issue, pages | Nucleic Acids Res, Vol. 49, Issue 8, Page 4599-4612, Year 2021 |
| Publish date | May 7, 2021 |
 Authors | Keisuke Oki / Takeshi Yamagami / Mariko Nagata / Kouta Mayanagi / Tsuyoshi Shirai / Naruhiko Adachi / Tomoyuki Numata / Sonoko Ishino / Yoshizumi Ishino /  |
| PubMed 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 ...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. |
 External links | Nucleic Acids Res / PubMed:33849056 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 7.1 Å |
| Structure data |  EMDB-30937: |
| Source |
|
Thermococcus kodakarensis KOD1 (archaea)