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• W2019342009 startingPage "2724" @default.
• W2019342009 abstract "In PCR, DNA polymerases from thermophilic bacteria catalyze the extension of primers annealed to templates as well as the structure-specific cleavage of the products of primer extension. Here we show that cleavage by Thermus aquaticus and Thermus thermophilus DNA polymerases can be precise and substantial: it occurs at the base of the stem-loop structure assumed by the single strand products of primer extension using as template a common genetic element, the promoter-operator of the Escherichia coli lactose operon, and may involve up to 30% of the products. The cleavage is independent of primer, template, and triphosphates, is dependent on substrate length and temperature, requires free ends and Mg2+, and is absent in DNA polymerases lacking the 5'-->3' exonuclease, such as the Stoffel fragment and the T7 DNA polymerase. Heterogeneity of the extension products results also from premature detachment of the enzyme approaching the 5' end of the template." @default.
• W2019342009 created "2016-06-24" @default.
• W2019342009 creator A5023050360 @default.
• W2019342009 creator A5027949460 @default.
• W2019342009 creator A5039525663 @default.
• W2019342009 date "1996-04-02" @default.
• W2019342009 modified "2023-09-26" @default.
• W2019342009 title "Heterogeneity of primer extension products in asymmetric PCR is due both to cleavage by a structure-specific exo/endonuclease activity of DNA polymerases and to premature stops." @default.
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• W2019342009 doi "https://doi.org/10.1073/pnas.93.7.2724" @default.
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