Collision with duplex DNA renders Escherichia coli DNA polymerase III holoenzyme susceptible to DNA polymerase IV-mediated polymerase switching on the sliding clamp

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A dynamic polymerase exchange with Escherichia coli DNA polymerase IV replacing DNA polymerase III on the sliding clamp.

An assay that measures synchronized, processive DNA replication by Escherichia coli DNA polymerase III holoenzyme was used to reveal replacement of pol III by the specialized lesion bypass DNA polymerase IV when the replicative polymerase is stalled. When idled replication is restarted, a rapid burst of pol III-catalyzed synthesis accompanied by approximately 7-kb full-length products is strong...

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DNA polymerases that duplicate chromosomes are remarkably processive multiprotein machines. These replicative polymerases remain in continuous association with the DNA over tens to hundreds of kilobases. What is the chemical basis of their strong grip to the template? The mystery behind the high processivity of the replicative polymerase of the Escherichia coli chromosome, DNA polymerase III ho...

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DNA polymerase III holoenzyme of Escherichia coli.

DNA polymerase III holoenzyme has been purified from Escherichia coli HMS-83, using, as an assay, the conversion of coliphage G4 single-stranded DNA to the duplex replicative form. The holoenzyme consists of at least four different subunits: a, /I, y, and 6 of 140,000, 40,000, 52,000, and 32,000 daltons, respectively. The (Y subunit is DNA polymerase III, the dnaE gene product. The holoenzyme h...

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Interplay of clamp loader subunits in opening the beta sliding clamp of Escherichia coli DNA polymerase III holoenzyme.

The Escherichia coli beta dimer is a ring-shaped protein that encircles DNA and acts as a sliding clamp to tether the replicase, DNA polymerase III holoenzyme, to DNA. The gamma complex (gammadeltadelta'chipsi) clamp loader couples ATP to the opening and closing of beta in assembly of the ring onto DNA. These proteins are functionally and structurally conserved in all cells. The eukaryotic equi...

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DNA Polymerase III of Escherichia coli

DNA polymerase III, the core of the DNA polymerase III holoenzyme, has been purified Z&000-fold to 97% homogeneity from Escherichiu coli HMS-83. The enzyme contains three subunits: (Y, E, and 0 of 140,000, 25,000, and 10,000 daltons, respectively. The cy subunit has been previously shown to be a component of both DNA polymerase III and the more complex DNA polymerase III holoenzyme (Livingston,...

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ژورنال

عنوان ژورنال: Scientific Reports

سال: 2017

ISSN: 2045-2322

DOI: 10.1038/s41598-017-13080-1