The DNA polymerase III holoenzyme contains γ and is not a trimeric polymerase

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The DNA polymerase III holoenzyme contains γ and is not a trimeric polymerase.

There is widespread agreement that the clamp loader of the Escherichia coli replicase has the composition DnaX3δδ'χψ. Two DnaX proteins exist in E. coli, full length τ and a truncated γ that is created by ribosomal frameshifting. τ binds DNA polymerase III tightly; γ does not. There is a controversy as to whether or not DNA polymerase III holoenzyme (Pol III HE) contains γ. A three-τ form of Po...

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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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The sliding clamp of DNA polymerase III holoenzyme encircles DNA.

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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Assembly and disassembly of DNA polymerase holoenzyme.

The complex task of genomic replication requires a large collection of proteins properly assembled within the close confines of the replication fork. The mechanism and dynamics of holoenzyme assembly and disassembly have been investigated using steady state and pre-steady state methods as opposed to structural studies, primarily due to the intrinsic transient nature of these protein complexes d...

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The 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: Nucleic Acids Research

سال: 2016

ISSN: 0305-1048,1362-4962

DOI: 10.1093/nar/gkv1510