PCNA accelerates the nucleotide incorporation rate by DNA polymerase δ
Abstract DNA polymerase delta (Pol δ) is responsible for the elongation and maturation of Okazaki fragments in eukaryotic cells. Proliferating cell nuclear antigen (PCNA) recruits Pol δ to the DNA and serves as a processivity factor. Here, we show that PCNA also stimulates the catalytic rate of Sacc...
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| Published in: | Nucleic acids research Vol. 47; no. 4; pp. 1977 - 1986 |
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28-02-2019
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| Abstract | Abstract
DNA polymerase delta (Pol δ) is responsible for the elongation and maturation of Okazaki fragments in eukaryotic cells. Proliferating cell nuclear antigen (PCNA) recruits Pol δ to the DNA and serves as a processivity factor. Here, we show that PCNA also stimulates the catalytic rate of Saccharomyces cerevisiae Pol δ by >10-fold. We determined template/primer DNA binding affinities and stoichiometries by Pol δ in the absence of PCNA, using electrophoretic mobility shift assays, fluorescence intensity changes and fluorescence anisotropy binding titrations. We provide evidence that Pol δ forms higher ordered complexes upon binding to DNA. The Pol δ catalytic rates in the absence and presence of PCNA were determined at millisecond time resolution using quench flow kinetic measurements. The observed rate for single nucleotide incorporation by a preformed DNA-Pol δ complex in the absence of PCNA was 40 s−1. PCNA enhanced the nucleotide incorporation rate by >10 fold. Compared to wild-type, a growth-defective yeast PCNA mutant (DD41,42AA) showed substantially less stimulation of the Pol δ nucleotide incorporation rate, identifying the face of PCNA that is important for the acceleration of catalysis. |
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| AbstractList | Abstract
DNA polymerase delta (Pol δ) is responsible for the elongation and maturation of Okazaki fragments in eukaryotic cells. Proliferating cell nuclear antigen (PCNA) recruits Pol δ to the DNA and serves as a processivity factor. Here, we show that PCNA also stimulates the catalytic rate of Saccharomyces cerevisiae Pol δ by >10-fold. We determined template/primer DNA binding affinities and stoichiometries by Pol δ in the absence of PCNA, using electrophoretic mobility shift assays, fluorescence intensity changes and fluorescence anisotropy binding titrations. We provide evidence that Pol δ forms higher ordered complexes upon binding to DNA. The Pol δ catalytic rates in the absence and presence of PCNA were determined at millisecond time resolution using quench flow kinetic measurements. The observed rate for single nucleotide incorporation by a preformed DNA-Pol δ complex in the absence of PCNA was 40 s−1. PCNA enhanced the nucleotide incorporation rate by >10 fold. Compared to wild-type, a growth-defective yeast PCNA mutant (DD41,42AA) showed substantially less stimulation of the Pol δ nucleotide incorporation rate, identifying the face of PCNA that is important for the acceleration of catalysis. DNA polymerase delta (Pol δ) is responsible for the elongation and maturation of Okazaki fragments in eukaryotic cells. Proliferating cell nuclear antigen (PCNA) recruits Pol δ to the DNA and serves as a processivity factor. Here, we show that PCNA also stimulates the catalytic rate of Saccharomyces cerevisiae Pol δ by >10-fold. We determined template/primer DNA binding affinities and stoichiometries by Pol δ in the absence of PCNA, using electrophoretic mobility shift assays, fluorescence intensity changes and fluorescence anisotropy binding titrations. We provide evidence that Pol δ forms higher ordered complexes upon binding to DNA. The Pol δ catalytic rates in the absence and presence of PCNA were determined at millisecond time resolution using quench flow kinetic measurements. The observed rate for single nucleotide incorporation by a preformed DNA-Pol δ complex in the absence of PCNA was 40 s-1. PCNA enhanced the nucleotide incorporation rate by >10 fold. Compared to wild-type, a growth-defective yeast PCNA mutant (DD41,42AA) showed substantially less stimulation of the Pol δ nucleotide incorporation rate, identifying the face of PCNA that is important for the acceleration of catalysis. DNA polymerase delta (Pol δ) is responsible for the elongation and maturation of Okazaki fragments in eukaryotic cells. Proliferating cell nuclear antigen (PCNA) recruits Pol δ to the DNA and serves as a processivity factor. Here, we show that PCNA also stimulates the catalytic rate of Saccharomyces cerevisiae Pol δ by >10-fold. We determined template/primer DNA binding affinities and stoichiometries by Pol δ in the absence of PCNA, using electrophoretic mobility shift assays, fluorescence intensity changes and fluorescence anisotropy binding titrations. We provide evidence that Pol δ forms higher ordered complexes upon binding to DNA. The Pol δ catalytic rates in the absence and presence of PCNA were determined at millisecond time resolution using quench flow kinetic measurements. The observed rate for single nucleotide incorporation by a preformed DNA-Pol δ complex in the absence of PCNA was 40 s −1 . PCNA enhanced the nucleotide incorporation rate by >10 fold. Compared to wild-type, a growth-defective yeast PCNA mutant (DD41,42AA) showed substantially less stimulation of the Pol δ nucleotide incorporation rate, identifying the face of PCNA that is important for the acceleration of catalysis. |
| Author | Mondol, Tanumoy Galletto, Roberto Stodola, Joseph L Burgers, Peter M |
| AuthorAffiliation | 2 MilliporeSigma, St. Louis, MO, USA 1 Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO, USA |
| AuthorAffiliation_xml | – name: 2 MilliporeSigma, St. Louis, MO, USA – name: 1 Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO, USA |
| Author_xml | – sequence: 1 givenname: Tanumoy surname: Mondol fullname: Mondol, Tanumoy organization: Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO, USA – sequence: 2 givenname: Joseph L surname: Stodola fullname: Stodola, Joseph L organization: Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO, USA – sequence: 3 givenname: Roberto surname: Galletto fullname: Galletto, Roberto organization: Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO, USA – sequence: 4 givenname: Peter M surname: Burgers fullname: Burgers, Peter M email: burgers@biochem.wustl.edu organization: Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30605530$$D View this record in MEDLINE/PubMed |
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DNA polymerase delta (Pol δ) is responsible for the elongation and maturation of Okazaki fragments in eukaryotic cells. Proliferating cell nuclear... DNA polymerase delta (Pol δ) is responsible for the elongation and maturation of Okazaki fragments in eukaryotic cells. Proliferating cell nuclear antigen... |
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| StartPage | 1977 |
| SubjectTerms | Catalysis DNA - genetics DNA Polymerase III - genetics DNA Primers - genetics DNA Replication - genetics DNA-Binding Proteins - genetics Nucleic Acid Enzymes Proliferating Cell Nuclear Antigen - genetics Protein Binding Saccharomyces cerevisiae - genetics |
| Title | PCNA accelerates the nucleotide incorporation rate by DNA polymerase δ |
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