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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 alpha subunit of Escherichia coli DNA polymerase III a capacity for highly processive DNA synthesis and stable binding to primer/template DNA. Research Abstract Details 

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  • 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. Abstract Text:

    fusamitsu yanagiharaFusamitsu Yanagihara,shohei yoshidaShohei Yoshida,yutaka sugayaYutaka Sugaya,hisaji makiHisaji Maki,fusamitsu yanagiharaFusamitsu Yanagihara,shohei yoshidaShohei Yoshida,yutaka sugayaYutaka Sugaya,hisaji makiHisaji Maki,

    The strong mutator mutation dnaE173 which causes an amino-acid substitution in the alpha 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 beta-clamp subunit. Here we show that, in contrast to distributive DNA synthesis exhibited by wild-type alpha subunit, the dnaE173 mutant form of alpha subunit catalyzes highly processive DNA chain elongation without the aid of the beta-clamp. More surprisingly, the dnaE173 alpha subunit appeared to form a stable complex with primer/template DNA, while no such affinity was detected with wild-type alpha subunit. We consider that the highly increased affinity of alpha 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.

    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. Publishing Authors By Initials

    f yanagiharaF Yanagihara,s yoshidaS Yoshida,y sugayaY Sugaya,h makiH Maki,f yanagiharaF Yanagihara,s yoshidaS Yoshida,y sugayaY Sugaya,h makiH Maki,

    For similar abstracts research abstracts see: abstracts research

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    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. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Genes & genetic systems

    VOLUME: 82

    Page Numbers: 273-80

    Journal Abbreviation: Genes Genet. Syst.

    ISSN: 1341-7568

    DAY: 26

    MONTH: Aug

    YEAR: 2007

    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. Information

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    LANGUAGE: eng

    NlmUniqueID: 9607822

    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. Keywords Mesh Terms:

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    Grant and Affiliation Information for 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.

    AFFILIATION: Department of Molecular Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara, Japan.

    Country: Japan

    Japan Research PublicationJapan Research Publication

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    MEDLINETA: Genes Genet Syst

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    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 Related Publications

     

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