ArticleNucleic acids research2009
A trimeric DNA polymerase complex increases the native replication processivity.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- 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
- PCNA accelerates the nucleotide incorporation rate by DNA polymerase δ.Nucleic acids research · 2019Article
- Increased Processivity, Misincorporation, and Nucleotide Incorporation Efficiency in Sulfolobus solfataricus Dpo4 Thumb Domain Mutants.Applied and environmental microbiology · 2017Article
- Characterization of a coupled DNA replication and translesion synthesis polymerase supraholoenzyme from archaea.Nucleic acids research · 2017Article
- Sulfolobus replication factor C stimulates the activity of DNA polymerase B1.Journal of bacteriology · 2014Article
- Structure of a highly conserved domain of Rock1 required for Shroom-mediated regulation of cell morphology.PloS one · 2013Article
- Differential temperature-dependent multimeric assemblies of replication and repair polymerases on DNA increase processivity.Biochemistry · 2012Article
- Kinetics and fidelity of polymerization by DNA polymerase III from Sulfolobus solfataricus.Biochemistry · 2012Article
- Steric exclusion and wrapping of the excluded DNA strand occurs along discrete external binding paths during MCM helicase unwinding.Nucleic acids research · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
DNA polymerases are essential enzymes in all domains of life for both DNA replication and repair. The primary DNA replication polymerase from Sulfolobus solfataricus (SsoDpo1) has been shown previously to provide the necessary polymerization speed and exonuclease activity to replicate the genome accurately. We find that this polymerase is able to physically associate with itself to form a trimer and that this complex is stabilized in the presence of DNA. Analytical gel filtration and electrophoretic mobility shift assays establish that initially a single DNA polymerase binds to DNA followed by the cooperative binding of two additional molecules of the polymerase at higher concentrations of the enzyme. Protein chemical crosslinking experiments show that these are specific polymerase-polymerase interactions and not just separate binding events along DNA. Isothermal titration calorimetry and fluorescence anisotropy experiments corroborate these findings and show a stoichiometry where three polymerases are bound to a single DNA substrate. The trimeric polymerase complex significantly increases both the DNA synthesis rate and the processivity of SsoDpo1. Taken together, these results suggest the presence of a trimeric DNA polymerase complex that is able to synthesize long DNA strands more efficiently than the monomeric form.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.