Nucleoside triphosphate binding to DNA polymerase III holoenzyme of Escherichia coli. A direct photoaffinity labeling study.
نویسندگان
چکیده
منابع مشابه
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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We have used two self-annealing template-primers (TPs) to covalently cross-link the Klenow fragment of Escherichia coli DNA polymerase I in its polymerase mode. The specificity of cross-linking is demonstrated by the observation that other template-primers, but not the template or primer alone, readily compete with self-annealing TPs. The enzyme-TP covalent complex is catalytically active and c...
متن کاملDynamics of DNA polymerase III holoenzyme of Escherichia coli in replication of a multiprimed template.
Movements of DNA polymerase III holoenzyme (holoenzyme) in replicating a template multiprimed with synthetic pentadecadeoxynucleotides (15-mers) annealed at known positions on a single-stranded circular or linear DNA have been analyzed. After extension of one 15-mer on a multiprimed template, holoenzyme moves downstream in the direction of chain elongation to the next primer. Holoenzyme readily...
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The Escherichia coli gamma complex serves as a clamp loader, catalyzing ATP-dependent assembly of beta protein clamps onto primed DNA templates during DNA replication. These ring-shaped clamps tether DNA polymerase III holoenzyme to the template, facilitating rapid and processive DNA synthesis. This report focuses on the role of ATP binding and hydrolysis catalyzed by the gamma complex during c...
متن کاملThe gamma subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting.
The tau and gamma subunits of DNA polymerase III holoenzyme are both products of the dnaX gene. Since tau and gamma are required as stoichiometric components of the replicative complex, a mechanism must exist for the cell to coordinate their synthesis and ensure that both subunits are present in an adequate quantity and ratio for assembly. We have proposed that gamma is produced by a translatio...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1984
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)42890-0