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- W2013601176 abstract "DNA helicases are multi-functional motor proteins catalysing DNA unwinding using the energy derived from ATP hydrolysis. The monomeric bacterial helicase PcrA is one of the most characterized and it is known to unwinding DNA, moving one base per ATP. PcrA and the plasmid encoded replication initiator protein, RepD, act together during plasmid replication. RepD is a dimer and binds to a specific origin sequence containing inverted complementary repeat (ICR) elements. RepD binds to these elements and then nicks at a specific site exposing a single stranded region. PcrA helicase then binds to the ssDNA and begins unwinding. We have used a combination of high resolution optical tweezers and total internal reflection fluorescence microscopy to measure PcrA helicase activity. A DNA substrate, containing the ICR elements and a 5' biotin, was bound to a bead. Following incubation with RepD, the DNA complex binds to the helicase which is immobilized on the flow cell surface. Optical tweezers can be used in a passive state to measure unwinding rates or in a force feedback mode to measure stalling forces. Our experimental design allows us to look at finer details such as DNA slipping and the effect of DNA sequences on unwinding rates. Supported by DFG, SFB 863, Freidrich Baur-Stiftung and EMBO." @default.
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- W2013601176 date "2011-02-01" @default.
- W2013601176 modified "2023-09-26" @default.
- W2013601176 title "Single Molecule Fluorescence and Force Measurements on PcrA Helicase" @default.
- W2013601176 doi "https://doi.org/10.1016/j.bpj.2010.12.598" @default.
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