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    Temperature-dependent mutational specificity of an Escherichia coli mutator, dnaQ49, defective in 3'---> 5' exonuclease (proofreading) activity
    Roberta J. Isbell
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    Keywords:
    Proofreading
    Topics:
    DNA Repair Mechanisms
    CRISPR and Genetic Engineering
    Bacterial Genetics and Biotechnology
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    Structure and function of the proofreading exonuclease subunit of E. coli DNA polymerase III and related enzymes
    Ah Young Park
    Proofreading
    Klenow fragment
    RecBCD
    DNA polymerase II
    Citations (0)
    Nucleotide excision by E. coli DNA polymerase I in proofreading and non-proofreading modes
    Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression (1988)
    Philippe LecomteJacques Ninio
    Proofreading
    Processivity
    Primer (cosmetics)
    Klenow fragment
    DNA clamp
    DNA polymerase I
    DNA polymerase II
    Citations (4)
    Snapshots of the Structure and Function of Two Binuclear Metallohydrolases: The Proofreading 3'-5' Exonuclease Subunit of Escherichia coli DNA Polymerase III and the Purple Scid Phosphatase from Sweet Potato
    Nataša MitićC J NobleNicholas E. DixonGraeme R. HansonGerhard Schenk
    Proofreading
    Citations (0)
    Mutagenic DNA repair in Escherichia coli XIII Proofreading exonuclease of DNA polymerase III holoenzyme is not operational during UV mutagenesis
    Mutation Research/DNA Repair Reports (1987)
    Roger WoodgateB.A. BridgesGuadalupe HerreraManuel Blanco
    Proofreading
    Klenow fragment
    DNA polymerase I
    RecBCD
    Citations (42)
    On the fidelity of DNA replication: herpes DNA potymerase and its associated exonuclease
    Nucleic Acids Research (1987)
    John AbbottsYukihiro NishiyamaShonen YoshidaLawrence A. Loeb
    Procaryotic DNA polymerases contain an associated 3'----5' exonuclease activity which provides a proofreading function and contributes substantially to replication fidelity. DNA polymerases of the eucaryotic herpes-type viruses contain similar associated exonuclease activities. We have investigated the fidelity of polymerases purified from wild type herpes simplex virus, as well as from mutator and antimutator strains. On synthetic templates, the herpes enzymes show greater relative exonuclease activities, and greater ability to excise a terminal mismatched base, than procaryotic DNA polymerases which proofread. On a phi X174 natural DNA template, the herpes enzymes are more accurate than purified eucaryotic DNA polymerases; the error rate is similar to E. coli polymerase I. However, conditions which abnegate proofreading by E. coli polymerase I have little effect on the herpes enzymes. We conclude that either these viral polymerases are accurate in the absence of proofreading, or the conditions examined have little effect on proofreading by the herpes DNA polymerases.
    Proofreading
    DNA polymerase II
    Klenow fragment
    DNA clamp
    DNA polymerase I
    Primer (cosmetics)
    Primase
    Citations (19)
    Temperature-dependent mutational specificity of an Escherichia coli mutator, dnaQ49, defective in 3'---> 5' exonuclease (proofreading) activity
    Roberta J. Isbell
    Proofreading
    Citations (0)
    Thermostable Bst DNA polymerase I lacks a 3′ → 5′ proofreading exonuclease activity
    Genetic Analysis Biomolecular Engineering (1996)
    J Aliotta
    Proofreading
    Klenow fragment
    DNA polymerase II
    DNA clamp
    Primer (cosmetics)
    Citations (4)
    Theory of the proofreading mechanism of DNA Polymerase: a new kinetic model with higher-order terminal effects
    arXiv (Cornell University) (2016)
    Yongshun SongYao-Gen ShuXin ZhouZhong-Can Ou-YangMing Li
    The fidelity of DNA replication by DNA polymerase (DNAP) has long been an important issue in basic researches and application studies in biology. While numerous experiments have revealed details of the molecular structure and working mechanism of DNAP, theoretical studies of the fidelity issue are still lacking. Kinetic models which considered explicitly both the polymerase pathway and the exonuclease (proofreading) pathway were proposed since 1970s', but so far there was no rigorous treatment of such models. In this paper, we propose a new kinetic model of the exonuclease proofreading mechanism, based on some recent experimental observations. We present a rigorous analytical treatment of the steady-state kinetic equations including higher-order terminal effects, and then apply the results to the fidelity problem of some real DNAPs. Our results show good agreements with previous intuitive estimate of some DNAPs' fidelity under bio-relevant conditions.
    Proofreading
    Citations (0)
    Kinetics and thermodynamics of DNA polymerases with exonuclease proofreading
    Physical review. E (2016)
    Pierre Gaspard
    Kinetic theory and thermodynamics are applied to DNA polymerases with exonuclease activity, taking into account the dependence of the rates on the previously incorportated nucleotide. The replication fidelity is shown to increase significantly thanks to this dependence at the basis of the mechanism of exonuclease proofreading. In particular, this dependence can provide up to a hundred-fold lowering of the error probability under physiological conditions. Theory is compared with numerical simulations for the DNA polymerases of T7 viruses and human mitochondria.
    Proofreading
    Citations (17)
    Age dependent decline in the 3′→5′ exonuclease activity involved in proofreading during DNA synthesis
    Mechanisms of Ageing and Development (1998)
    Takahiko TaguchiMitsugu FukudaTosifusa TodaMochihiko Ohashi
    Proofreading
    Primer (cosmetics)
    Klenow fragment
    Exonuclease III
    DNA polymerase II
    Citations (5)