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Browsing by Subject "T2"

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  • Ojalehto, Tuomas (2016)
    Proteins responsible for homologous recombination are collectively called recombinases. They also have an important role in maintaining genome integrity. Recombinases are found in all three kingdoms of life. The first identified and characterized recombinase was RecA from Escherichia coli. Recombinases exhibit ATP hydrolysis coupled DNA-binding activity and strand exchange activities during homologous recombination. Homologous recombination produces new genetic combinations for evolution and general way to describe the different steps of homologous recombination is a DSBR model. Homologous recombination occurs in eukaryotic and prokaryotic cells during meiosis crossover and horizontal gene transfer, respectively. The homologous recombination machineries are remarkably complex and synergistic and much is not known about detailed mechanisms for a majority of the species. More recently, recombinases have been used in isothermal nucleic acid amplification methods, mainly in recombinase polymerase amplification RPA and strand invasion based amplification SIBA. The aim of this study was to identify, clone, produce and analyze the functionality of novel recombinases from bacteria and viruses. The acitivity for single-stranded DNA binding and strand exchange was studied. The compatibility of the produced recombinases in strand invasion based amplification SIBA method was evaluated. Two recombinases from Enterobacteria phages T2 and RB69 were found to be functional and compatible in three SIBA assays.