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- W2104239241 abstract "Helicases are ATP-dependent enzymes that use the structural changes induced by ATP binding, hydrolysis and release to unwind double stranded nucleic acids. We have studied the structural transitions of partial duplex DNA bound E-coli Rep helicase monomer by in vitro single molecule Förster resonance energy transfer (FRET) methodology. Constrained triangulation procedures were applied globally on FRET measurements from eight Rep mutants, donor labeled at different residues, and three DNA substrates, acceptor labeled at different nucleotides on duplex, to study these conformational states. A total of 96 different measurements were performed and used in the triangulation analysis. Such over-sampling reduces the likelihood of a single site with unusual photophysical properties to negatively impact the results. Our results show that binding of ATPγS to Rep induces a large conformational change which is then reversed in two approximately equal steps during ATP dephosphorylation (ATP to ADP.Pi transition) and ADP release. We do not observe a significant conformational change upon phosphate release (ADP.Pi to ADP transition). The large conformational change upon ATPγS binding is consistent with the rotation of the Rep domains in a direction that brings them closer to the duplex. In addition, we show that Rep has a preference to bind to ssDNA/dsDNA junction compared to the other sites along the ssDNA. Finally, we show that Rep remains in the closed conformation during all ATP hydrolysis intermediates when bound to the vicinity of ssDNA/dsDNA junction. Our studies not only reveal the structural transitions of Rep helicase-partial duplex DNA complex during ATP hydrolysis cycle but also demonstrate the potential of triangulation analysis as a versatile single molecule technique for probing structural information in physiological conditions." @default.
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- W2104239241 date "2009-02-01" @default.
- W2104239241 modified "2023-09-28" @default.
- W2104239241 title "Structural Transitions Of a Helicase-Partial Duplex DNA Complex during ATP Hydrolysis Cycle" @default.
- W2104239241 doi "https://doi.org/10.1016/j.bpj.2008.12.2120" @default.
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