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a: template, b: leading strand, c: lagging strand, d: replication fork, e: primer, f: Okazaki fragments Many enzymes are involved in the DNA replication fork. The replication fork is a structure that forms within the long helical DNA during DNA replication.
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 ...
Being the primary holoenzyme involved in replication activity, the DNA Pol III holoenzyme also has proofreading capabilities that corrects replication mistakes by means of exonuclease activity reading 3'→5' and synthesizing 5'→3'. DNA Pol III is a component of the replisome, which is located at the replication fork.
During DNA replication, the double helix is unwound and the complementary strands are separated by the enzyme DNA helicase, creating what is known as the DNA replication fork. Following this fork, DNA primase and DNA polymerase begin to act in order to create a new complementary strand.
Topoisomerase is the enzyme that aids in the unzipping and recombination of the double-helix. Specifically, topoisomerase prevents the double-helix from supercoiling, or becoming too tightly wound. Three topoisomerase enzymes are involved in this process: Type IA Topoisomerase, Type IB Topoisomerase, and Type II Topoisomerase. [9]
Eukaryotic DNA replication is a conserved ... These enzymes move along single-stranded DNA and ... In vivo, it is the main polymerase involved in both ...
The replication of bacteriophage T4 DNA upon infection of E. coli is a well-studied DNA replication system. During the period of exponential DNA increase at 37°C, the rate of elongation is 749 nucleotides per second. [11] The mutation rate during replication is 1.7 mutations per 10 8 base pairs. [12]
DNA polymerase I (or Pol I) is an enzyme that participates in the process of prokaryotic DNA replication. Discovered by Arthur Kornberg in 1956, [1] it was the first known DNA polymerase (and the first known of any kind of polymerase). It was initially characterized in E. coli and is ubiquitous in prokaryotes.