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The replication fork is a structure that forms within the long helical DNA during DNA replication. It is produced by enzymes called helicases that break the hydrogen bonds that hold the DNA strands together in a helix. The resulting structure has two branching "prongs", each one made up of a single strand of DNA.
RecQ is a family of DNA helicase enzymes that are found in various organisms including bacteria, archaea, and eukaryotes (like humans). These enzymes play important roles in DNA metabolism during DNA replication, recombination, and repair. There are five known RecQ helicase proteins in humans: RecQ1, BLM, WRN, RecQ4, and RecQ5.
The process of semiconservative replication for the site of DNA replication is a fork-like DNA structure, the replication fork, where the DNA helix is open, or unwound, exposing unpaired DNA nucleotides for recognition and base pairing for the incorporation of free nucleotides into double-stranded DNA.
Although RNA enzymes were discovered before DNA enzymes, the latter have some distinct advantages. DNA is more cost-effective, and DNA can be made with longer sequence length and can be made with higher purity in solid-phase synthesis. [30] Several studies have shown the usage of DNAzymes to inhibit influenza A and B virus replication in host ...
A DNA polymerase is a member of a family of enzymes that catalyze the synthesis of DNA molecules from nucleoside triphosphates, the molecular precursors of DNA. These enzymes are essential for DNA replication and usually work in groups to create two identical DNA duplexes from a single original DNA duplex. During this process, DNA polymerase ...
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 gyrase, or simply gyrase, is an enzyme within the class of topoisomerase and is a subclass of Type II topoisomerases [1] that reduces topological strain in an ATP dependent manner while double-stranded DNA is being unwound by elongating RNA-polymerase [2] or by helicase in front of the progressing replication fork.
The structure of the Toprim fold and DNA-binding core of yeast topoisomerase II was first solved by Berger and Wang, [12] and the first gyrase DNA-binding core was solved by Morais Cabral et al. [13] The structure solved by Berger revealed important insights into the function of the enzyme. The DNA-binding core consists of the WHD, which leads ...