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Cited by 39Evolution and Genetic DynamicsBacteriophages and microbial interactionsDNA Repair Mechanisms

Dissecting the Fidelity of Bacteriophage RB69 DNA Polymerase: Site-Specific Modulation of Fidelity by Polymerase Accessory Proteins

Bebenek, Anna, Carver, Geraldine T, Dressman, Holly Kloos, Kadyrov, Farid A, Haseman, Joseph K, Petrov, Vasiliy, Konigsberg, William H, Karam, Jim D +1 more·2002·Genetics
DOI 10.1093/genetics/162.3.1003
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Abstract

Bacteriophage RB69 encodes a replicative B-family DNA polymerase (RB69 gp43) with an associated proofreading 3′ exonuclease. Crystal structures have been determined for this enzyme with and without DNA substrates. We previously described the mutation rates and kinds of mutations produced in vivo by the wild-type (Pol+ Exo+) enzyme, an exonuclease-deficient mutator variant (Pol+ Exo-), mutator variants with substitutions at Tyr567 in the polymerase active site (PolM Exo+), and the double mutator PolM Exo-. Comparing the mutational spectra of the Pol+ Exo- and Pol+ Exo+ enzymes revealed the patterns and efficiencies of proofreading, while Tyr567 was identified as an important determinant of base-selection fidelity. Here, we sought to determine how well the fidelities of the same enzymes are reflected in vitro. Compared to their behavior in vivo, the three mutator polymerases exhibited modestly higher mutation rates in vitro and their mutational predilections were also somewhat different. Although the RB69 gp43 accessory proteins exerted little or no effect on total mutation rates in vitro, they strongly affected mutation rates at many specific sites, increasing some rates and decreasing others.

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  • Accessory proteins other than exonucleases have also been demonstrated to modulate the fidelity of DNA synthesis.

    “Accessory proteins other than exonucleases have also been demonstrated to modulate the fidelity of DNA synthesis (reviewed in Ref. 15, and see Ref. 54 and references therein).”

    From DNA Replication Fidelity (2004) · cites this paper as [54]

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Authors
Bebenek, A., Carver, G. T., Dressman, H. K., Kadyrov, F. A., Haseman, J. K., Petrov, V., Konigsberg, W. H., Karam, J. D., & Drake, J. W.
Affiliations
  • Laboratory of Molecular Genetics
  • National Institutes of Health (US)
  • Tulane University (US)
  • Yale University (US)
Corresponding author
Drake, John W
ORCID
Venue
Genetics
Publisher
Oxford University Press (OUP)
Published
2002-11-01
Volume
162
Issue
3
Pages
1003-1018
ISSN
  • 0016-6731 (ISSN-L)
  • 1943-2631
DOI
10.1093/genetics/162.3.1003
OpenAlex
W2132215545
Cited by
39
References
58
Citations by year
2023: 1 · 2020: 1 · 2018: 1 · 2015: 2 · 2014: 3 · 2013: 1
FWCI
1.24
Type
journal article
Language
en
Open access
closed
Licence
academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)
Locations
  • Genetics (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Evolution and Genetic Dynamics
  • Physical Sciences › Environmental Science › Ecology › Bacteriophages and microbial interactions
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Keywords
family B DNA polymerase, proofreading exonuclease, in vitro mutagenesis, mutation rate
MeSH terms
Base Sequence, DNA, DNA-Directed DNA Polymerase, Molecular Sequence Data, Mutation, Viral Proteins, Bacteriophage M13, In Vitro Techniques

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