ArticleThe Journal of biological chemistry2015
Yeast DNA polymerase ϵ catalytic core and holoenzyme have comparable catalytic rates.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Efficient discrimination against RNA-containing primers by human DNA polymerase ε.Scientific reports · 2022Article
- Structural and Molecular Kinetic Features of Activities of DNA Polymerases.International journal of molecular sciences · 2022Review
- Impact of Genome Reduction in Microsporidia.Experientia supplementum (2012) · 2022Article
- Kinetic investigation of the polymerase and exonuclease activities of human DNA polymerase ε holoenzyme.The Journal of biological chemistry · 2020Article
- POLE Mutation Spectra Are Shaped by the Mutant Allele Identity, Its Abundance, and Mismatch Repair Status.Molecular cell · 2020Article
- Plant DNA Polymerases.International journal of molecular sciences · 2019Review
- PCNA accelerates the nucleotide incorporation rate by DNA polymerase δ.Nucleic acids research · 2019Article
- A recurrent cancer-associated substitution in DNA polymerase ε produces a hyperactive enzyme.Nature communications · 2019Article
- Structural consequence of the most frequently recurring cancer-associated substitution in DNA polymerase ε.Nature communications · 2019Article
- Article
- The DNA Pol ϵ stimulatory activity of Mrc1 is modulated by phosphorylation.Cell cycle (Georgetown, Tex.) · 2018Article
- Diverse roles of Dpb2, the non-catalytic subunit of DNA polymerase ε.Current genetics · 2017Review
- Eukaryotic DNA Replication Fork.Annual review of biochemistry · 2017Review
- Strand displacement synthesis by yeast DNA polymerase ε.Nucleic acids research · 2016Article
- Resolving individual steps of Okazaki-fragment maturation at a millisecond timescale.Nature structural & molecular biology · 2016Article
- Evidence for the kinetic partitioning of polymerase activity on G-quadruplex DNA.Biochemistry · 2015Article
- Comparison of the kinetic parameters of the truncated catalytic subunit and holoenzyme of human DNA polymerase ɛ.DNA repair · 2015Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The holoenzyme of yeast DNA polymerase ϵ (Pol ϵ) consists of four subunits: Pol2, Dpb2, Dpb3, and Dpb4. A protease-sensitive site results in an N-terminal proteolytic fragment of Pol2, called Pol2core, that consists of the catalytic core of Pol ϵ and retains both polymerase and exonuclease activities. Pre-steady-state kinetics showed that the exonuclease rates on single-stranded, double-stranded, and mismatched DNA were comparable between Pol ϵ and Pol2core. Single-turnover pre-steady-state kinetics also showed that the kpol of Pol ϵ and Pol2core were comparable when preloading the polymerase onto the primer-template before adding Mg(2+) and dTTP. However, a global fit of the data over six sequential nucleotide incorporations revealed that the overall polymerization rate and processivity were higher for Pol ϵ than for Pol2core. The largest difference between Pol ϵ and Pol2core was observed when challenged for the formation of a ternary complex and incorporation of the first nucleotide. Pol ϵ needed less than 1 s to incorporate a nucleotide, but several seconds passed before Pol2core incorporated detectable levels of the first nucleotide. We conclude that the accessory subunits and the C terminus of Pol2 do not influence the catalytic rate of Pol ϵ but facilitate the loading and incorporation of the first nucleotide by Pol ϵ.
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