Kinetic Mechanism for the Formation of the Presynaptic Complex of the Bacterial Recombinase RecA
作者： Martine Defais , Emilie Phez , Neil P. Johnson
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摘要: RecA protein from Escherichia colicatalyzes DNA strand exchange during homologous recombination in a reaction that requires nucleoside triphosphate cofactor. In the first step of this polymerizes on single-stranded to form filament with stoichiometry three nucleotides/RecA monomer called presynaptic complex. We have used fluorescence anisotropy fluorescein-labeled oligonucleotide investigate complex formation. RecA-ATPγS bound by two-step process. Kinetic studies revealed an intermediate polymerization had greater mobility than final product filament. The was transformed into process independent concentration and temperature, k = 0.3 ± 0.1 min−1. This same rate as reported for isomerization ATPγS (Paulus, B. F., Bryant, F. R. (1997) Biochemistry 36, 7832–7838). Judging measurements, hydrodynamic properties similar mixed containing monomers without ATPγS. These results show can assume conformations different segmental mobilities could play role recombination.
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