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DNA polymerase III holoenzyme is the primary enzyme complex involved in prokaryotic DNA replication. It was discovered by Thomas Kornberg (son of Arthur Kornberg ) and Malcolm Gefter in 1970.
DNA polymerase III holoenzyme is the primary enzyme involved in DNA replication in E. coli and belongs to family C polymerases. It consists of three assemblies: the pol III core, the beta sliding clamp processivity factor, and the clamp-loading complex. The core consists of three subunits: α, the polymerase activity hub, ɛ, exonucleolytic ...
After assembly around the DNA, the beta subunits' affinity for the gamma subunit is replaced by an affinity for the alpha and epsilon subunits, which together create the complete holoenzyme. [7] [8] [9] DNA polymerase III is the primary enzyme complex involved in prokaryotic DNA replication.
Once priming is complete, DNA polymerase III holoenzyme is loaded into the DNA and replication begins. The catalytic mechanism of DNA polymerase III involves the use of two metal ions in the active site, and a region in the active site that can discriminate between deoxyribonucleotides and ribonucleotides.
The τ and γ subunits are part of the DNA polymerase III holoenzyme of prokaryotes. The protein family is characterized by the well-conserved first N-terminal domain, approx. 365 amino acids. The eukaryotic equivalent to the DNA clamp loader is replication factor C, with the subunits RFC1, RFC2, RFC3, RFC4, and RFC5.
In molecular biology, the δ (delta) subunit of DNA polymerase III is encoded by the holA gene in E. coli and other bacteria. Along with the γ, δ', χ, and ψ subunits that make up the core polymerase, and the β accessory proteins, the δ subunit is responsible for the high speed and processivity of polIII. [1] [2]
Multiple DNA polymerases have specialized roles in the DNA replication process. In E. coli, which replicates its entire genome from a single replication fork, the polymerase DNA Pol III is the enzyme primarily responsible for DNA replication and forms a replication complex with extremely high processivity.
DnaG recruits the replicative DNA polymerase III, and replication begins. In eukaryotes, MCM heterohexamer is phosphorylated by CDC7 and CDK, which displaces Cdc6 and recruits MCM10. MCM10 cooperates with MCM2-7 in the recruitment of Cdc45. Cdc45 then recruits key components of the replisome; the replicative DNA polymerase α and its primase ...