ArticlePLoS biology2019
Structure of the DP1-DP2 PolD complex bound with DNA and its implications for the evolutionary history of DNA and RNA polymerases.
Article in PLoS biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Archaeal family B DNA polymerase facilitates lagging strand DNA replication in the Thermococcales.Nucleic acids research · 2026Article
- Communication between DNA polymerases and Replication Protein A within the archaeal replisome.Nature communications · 2024Article
- Tail-tape-fused virion and non-virion RNA polymerases of a thermophilic virus with an extremely long tail.Nature communications · 2024Article
- Molecular basis for proofreading by the unique exonuclease domain of Family-D DNA polymerases.Nature communications · 2023Article
- Identification of WUSCHEL-related homeobox gene and truncated small peptides in transformation efficiency improvement in Eucalyptus.BMC plant biology · 2023Article
- Reclassification of family A DNA polymerases reveals novel functional subfamilies and distinctive structural features.Nucleic acids research · 2023Article
- Article
- Structural insights into the dual activities of the two-barrel RNA polymerase QDE-1.Nucleic acids research · 2022Article
- Structural and Molecular Kinetic Features of Activities of DNA Polymerases.International journal of molecular sciences · 2022Review
- Family D DNA polymerase interacts with GINS to promote CMG-helicase in the archaeal replisome.Nucleic acids research · 2022Article
- DNA polymerase D temporarily connects primase to the CMG-like helicase before interacting with proliferating cell nuclear antigen.Nucleic acids research · 2021Article
- Evolution of the genetic code.Transcription · 2021Review
- Phenotypic Characterization ofFrontiers in microbiology · 2021Article
- Early Evolution of Transcription Systems and Divergence of Archaea and Bacteria.Frontiers in molecular biosciences · 2021Review
- Structural Studies of HNA Substrate Specificity in Mutants of an Archaeal DNA Polymerase Obtained by Directed Evolution.Biomolecules · 2020Article
- Novel ribonucleotide discrimination in the RNA polymerase-like two-barrel catalytic core of Family D DNA polymerases.Nucleic acids research · 2020Article
- Review
- The LUCA and its complex virome.Nature reviews. Microbiology · 2020Review
- Two conformations of DNA polymerase D-PCNA-DNA, an archaeal replisome complex, revealed by cryo-electron microscopy.BMC biology · 2020Article
- Diversity and evolution of B-family DNA polymerases.Nucleic acids research · 2020Review
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10 authors.
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No grant is acknowledged in the PubMed record.
Abstract
PolD is an archaeal replicative DNA polymerase (DNAP) made of a proofreading exonuclease subunit (DP1) and a larger polymerase catalytic subunit (DP2). Recently, we reported the individual crystal structures of the DP1 and DP2 catalytic cores, thereby revealing that PolD is an atypical DNAP that has all functional properties of a replicative DNAP but with the catalytic core of an RNA polymerase (RNAP). We now report the DNA-bound cryo-electron microscopy (cryo-EM) structure of the heterodimeric DP1-DP2 PolD complex from Pyrococcus abyssi, revealing a unique DNA-binding site. Comparison of PolD and RNAPs extends their structural similarities and brings to light the minimal catalytic core shared by all cellular transcriptases. Finally, elucidating the structure of the PolD DP1-DP2 interface, which is conserved in all eukaryotic replicative DNAPs, clarifies their evolutionary relationships with PolD and sheds light on the domain acquisition and exchange mechanism that occurred during the evolution of the eukaryotic replisome.
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