The dnaE173 mutator mutation confers on the α subunit of Escherichia coli DNA polymerase 3 a capacity for highly processive DNA synthesis and stable binding to primer/template DNA

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  • Yanagihara Fusamitsu
    Department of Molecular Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology
  • Yoshida Shohei
    Department of Molecular Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology
  • Sugaya Yutaka
    Department of Molecular Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology
  • Maki Hisaji
    Department of Molecular Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology

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タイトル別名
  • The dnaE173 mutator mutation confers on the .ALPHA. subunit of Escherichia coli DNA polymerase III a capacity for highly processive DNA synthesis and stable binding to primer/template DNA
  • The dnaE173 mutator mutation confers on the アルファ subunit of Escherichia coli DNA polymerase 3 a capacity for highly processive DNA synthesis and stable binding to primer template DNA
  • The dnaE173 mutator mutation confers on the α subunit of Escherichia coli DNA polymerase III a capacity for highly processive DNA synthesis and stable binding to primer / template DNA

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説明

The strong mutator mutation dnaE173 which causes an amino-acid substitution in the α subunit of DNA polymerase III is unique in its ability to induce sequence-substitution mutations. We showed previously that multiple biochemical properties of DNA polymerase III holoenzyme of Escherichia coli are simultaneously affected by the dnaE173 mutation. These effects include a severely reduced proofreading capacity, an increased resistance to replication-pausing on the template DNA, a capability to readily promote strand-displacement DNA synthesis, a reduced rate of DNA chain elongation, and an ability to catalyze highly processive DNA synthesis in the absence of the β-clamp subunit. Here we show that, in contrast to distributive DNA synthesis exhibited by wild-type α subunit, the dnaE173 mutant form of α subunit catalyzes highly processive DNA chain elongation without the aid of the β-clamp. More surprisingly, the dnaE173 α subunit appeared to form a stable complex with primer/template DNA, while no such affinity was detected with wild-type α subunit. We consider that the highly increased affinity of α subunit for primer/template DNA is the basis for the pleiotropic effects of the dnaE173 mutation on DNA polymerase III, and provides a clue to the molecular mechanisms underlying sequence substitution mutagenesis.<br>

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