Genes & Genetic Systems
Online ISSN : 1880-5779
Print ISSN : 1341-7568
ISSN-L : 1341-7568
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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
Fusamitsu YanagiharaShohei YoshidaYutaka SugayaHisaji Maki
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2007 年 82 巻 4 号 p. 273-280

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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.

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© 2007 by The Genetics Society of Japan
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