ArticleNature communications2017
Identification and characterization of a heterotrimeric archaeal DNA polymerase holoenzyme.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Conserved and lineage-specific hypothetical proteins may have played a central role in the rise and diversification of major archaeal groups.BMC biology · 2022Article
- A Novel Family of Winged-Helix Single-Stranded DNA-Binding Proteins from Archaea.International journal of molecular sciences · 2022Article
- A Well-Conserved Archaeal B-Family Polymerase Functions as an Extender in Translesion Synthesis.mBio · 2022Article
- The combined DNA and RNA synthetic capabilities of archaeal DNA primase facilitate primer hand-off to the replicative DNA polymerase.Nature communications · 2022Article
- Searching for New Z-DNA/Z-RNA Binding Proteins Based on Structural Similarity to Experimentally Validated Zα Domain.International journal of molecular sciences · 2022Article
- DNA Polymerase B1 Binding Protein 1 Is Important for DNA Repair by Holoenzyme PolB1 in the Extremely Thermophilic CrenarchaeonMicroorganisms · 2021Article
- A hand-off of DNA between archaeal polymerases allows high-fidelity replication to resume at a discrete intermediate three bases past 8-oxoguanine.Nucleic acids research · 2020Article
- Archaeal DNA Replication.Annual review of microbiology · 2020Review
- The replication machinery of LUCA: common origin of DNA replication and transcription.BMC biology · 2020Article
- Structural basis for the increased processivity of D-family DNA polymerases in complex with PCNA.Nature communications · 2020Article
- A Unique B-Family DNA Polymerase Facilitating Error-Prone DNA Damage Tolerance in Crenarchaeota.Frontiers in microbiology · 2020Article
- PolB1 Is Sufficient for DNA Replication and Repair Under Normal Growth Conditions in the Extremely Thermophilic CrenarchaeonFrontiers in microbiology · 2020Article
- Translesion and Repair DNA Polymerases: Diverse Structure and Mechanism.Annual review of biochemistry · 2018Review
- Article
- Two Family B DNA Polymerases FromFrontiers in molecular biosciences · 2018Article
- Cultivation and Genomic Analysis of "Frontiers in microbiology · 2018Article
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Since their initial characterization over 30 years ago, it has been believed that the archaeal B-family DNA polymerases are single-subunit enzymes. This contrasts with the multi-subunit B-family replicative polymerases of eukaryotes. Here we reveal that the highly studied PolB1 from Sulfolobus solfataricus exists as a heterotrimeric complex in cell extracts. Two small subunits, PBP1 and PBP2, associate with distinct surfaces of the larger catalytic subunit and influence the enzymatic properties of the DNA polymerase. Thus, multi-subunit replicative DNA polymerase holoenzymes are present in all three domains of life. We reveal the architecture of the assembly by a combination of cross-linking coupled with mass spectrometry, X-ray crystallography and single-particle electron microscopy. The small subunits stabilize the holoenzyme assembly and the acidic tail of one small subunit mitigates the ability of the enzyme to perform strand-displacement synthesis, with important implications for lagging strand DNA synthesis.
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