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Phi29 DNA Polymerase, a Potent Amplification Enzyme

AuthorsSalas, Margarita ; Vega, Miguel de ; Lázaro, José M. ; Blanco, Luis
KeywordsPhage phi29
DNA polymerase
Bacillus Subtilis
Terminal protein
DNA replication
DNA synthesis
Issue Date2004
PublisherHorizon Biosciences
CitationDNA Amplification: Current Technologies and Applications: 21-34
Abstractø29 DNA polymerase is a 66 kDa monomeric DNA-dependent DNA polymerase responsible for all the mesophilic DNA synthesis reactions required to replicate the 19-kb-long linear dsDNA genome of bacteriophage ø29. To initiate replication at each DNA end, ø29 DNA polymerase catalyzes the incorporation of dAMP to a specific protein, the terminal protein (TP), which acts as a primer. Then, switching from TP-priming to DNA-priming occurs progressively, defining a transition stage in which TP still interacts with ø29 DNA polymerase. Once dissociated from TP, a single ø29 DNA polymerase molecule replicates each DNA strand without dissociation from the template, whereas it produces the displacement of the non-template strand. Due to these two specific properties of ø29 DNA polymerase: high processivity and strand-displacement ability, neither accessory proteins nor helicases are required for the elongating stage of ø29 DNA replication. From a more applied point of view, these two important properties of ø29 DNA polymerase, together with its high fidelity of DNA synthesis, form the basis for the application of this enzyme in an increasing number of in vitro procedures for isothermal DNA amplification.
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