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- W2048000788 abstract "Helicases catalyse the unwinding of double stranded DNA or RNA for a variety of functions through various mechanisms. The monomeric, bacterial helicase PcrA is well characterized: it translocates ssDNA with discrete steps of one base per ATP. The ATPase activity is enhanced by DNA and the cycle includes a rate limiting cleavage step, followed by rapid phosphate release. PcrA and the plasmid encoded replication initiator protein, RepD, act together during replication of some plasmids, containing antibiotic resistance. RepD is a dimer and binds to a specific origin sequence (ori) containing inverted complementary repeat (ICR) elements. ICRIII provides affinity and plasmid specificity, whereas ICRII is conserved amongst ori family members and contains the nick site for initiation. RepD binds to ICRIII and then nicks at a specific site in ICRII exposing a single-stranded region. PcrA helicase then binds to the ssDNA and begins unwinding. RepD has been shown to increase PcrA helicase activity; in the absence of RepD PcrA is a poor helicase. Measurements have shown that unwinding occurs at a reduced rate but the coupling ratio is unaltered. We have analyzed the mechanism of the PcrA ATPase cycle with ssDNA and extended this to include probing how DNA junctions and RepD affect this cycle. The individual rate constants were determined to see how RepD modulates the ATPase rate. This included utilizing the fluorescent ATP analogue mantATP to monitor fluorescence intensity in rapid-reaction, kinetic experiments, allowing the initial binding and release kinetics to be explored. The analogue was further used for analysis of the hydrolysis step using quenched-flow measurements. Additionally, the fluorescent phosphate binding protein (MDCC-PBP) independently measures the phosphate release step." @default.
- W2048000788 created "2016-06-24" @default.
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- W2048000788 date "2009-02-01" @default.
- W2048000788 modified "2023-10-16" @default.
- W2048000788 title "PcrA Helicase ATPase Mechanism: RepD Modulation During Unwinding" @default.
- W2048000788 doi "https://doi.org/10.1016/j.bpj.2008.12.2122" @default.
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