DNA unwinding enzyme II of Escherichia coli. 2. Characterization of the DNA unwinding activity.
The DNA-stimulated 75000-Mr ATPase described in the preceding paper is shown to be a further catalytic DNA unwinding principle (DNA unwinding enzyme II) made in Escherichia coli cells (the first being the 180000-Mr ATPase of the cells: DNA unwinding enzyme I). Unwinding depends strictly, on the supply of ATP. It occurs only under conditions permitting ATP dephosphorylation and it proceeds as long as enzyme molecules are permitted to enter the enzyme - DNA complex. The enzyme binds specifically to single-stranded DNA yielding a complex of only limited stability. These results are interpreted in terms of a distributive mode of action of the enzyme. It is argued that chain separation starts near a single-stranded DNA region and that, forced by continued adsorption of enzyme molecules to the DNA, it develops along the duplex. This mechanism is different from that deduced previously for DNA unwinding enzyme I. Complicated results were obtained using ATPase prepared from rep3 mutant cells.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D001667:Binding, Competitive; D004264:DNA Topoisomerases, Type I / Q000378:metabolism*; D004277:DNA, Single-Stranded; D004279:DNA, Viral; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D008970:Molecular Weight; D009690:Nucleic Acid Conformation; D013329:Structure-Activity Relationship
D004277:DNA, Single-Stranded; D004279:DNA, Viral; D000251:Adenosine Triphosphatases; D004264:DNA Topoisomerases, Type I