Abstract
The binding of the recA protein from E. coli to supercoiled double-stranded DNA is strongly dependent upon the superhelical density of the DNA molecule. A threshold of superhelical density is required for strong binding in the presence of ATP. This finding is consistent with a model in which recA protein first binds to unpaired regions and then polymerises on the contiguous double-stranded lattice.
MeSH terms
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Adenosine Triphosphate / analogs & derivatives
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Adenosine Triphosphate / pharmacology
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DNA, Superhelical / metabolism*
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Electrophoresis, Agar Gel
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Electrophoresis, Polyacrylamide Gel
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Nucleic Acid Conformation*
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Plasmids
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Rec A Recombinases / metabolism*
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Thionucleotides / pharmacology
Substances
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DNA, Superhelical
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Thionucleotides
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adenosine 5'-O-(3-thiotriphosphate)
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Adenosine Triphosphate
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Rec A Recombinases