Abstract: |
The rate of relaxation of supercoiled DNA by purified vaccinia topoisomerase I is stimulated 20-fold by 5 mM ATP. A similar effect is elicited by GTP, CTP, UTP, dATP, and adenosine 5'-(β,γ-imido)triphosphate. ATP-mediated rate enhancement requires salt as a coactivator. ADP and inorganic pyrophosphate also stimulate relaxation 10-20-fold, whereas AMP and inorganic phosphate have little effect. A model for allosteric activation of topoisomerase by nucleotides is suggested. |
Keywords: |
nonhuman; enzyme activation; enzyme activity; kinetics; escherichia coli; vaccinia virus; binding sites; dna topoisomerase; dna topoisomerases, type i; dna denaturation; magnesium; vaccinia; dna conformation; nucleotides; dna supercoiling; dna, superhelical; nucleoside triphosphate; salts; priority journal; article; support, non-u.s. gov't; support, u.s. gov't, p.h.s.
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