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- W1963485674 abstract "Using a fluorescent sensor for inorganic phosphate, the kinetics of ATP hydrolysis by PcrA helicase were measured in the presence of saturating concentrations of oligonucleotides of various lengths. There is a rapid phase of inorganic phosphate release that is equivalent to several turnovers of the ATPase, followed by slower steady-state ATP hydrolysis. The magnitude of the rapid phase is governed by the length of single-stranded DNA, while the slow phase is independent of its length. A kinetic model is presented in which the rapid phase is associated with translocation along single-stranded DNA, after the PcrA binds randomly along the DNA. There is a linear relationship between the length of single-stranded DNA and both the duration and amplitude of the rapid phase. These data suggest that the translocation activity occurs at 50 bases/s in unidirectional single-base steps, each requiring the hydrolysis of 1 ATP molecule." @default.
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- W1963485674 date "1999-12-09" @default.
- W1963485674 modified "2023-10-10" @default.
- W1963485674 title "Demonstration of Unidirectional Single-Stranded DNA Translocation by PcrA Helicase: Measurement of Step Size and Translocation Speed" @default.
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- W1963485674 doi "https://doi.org/10.1021/bi992105o" @default.
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