Selective inhibition of the dnase activity of the recBC enzyme by the DNA binding protein from Escherichia coli.
In the presence of the Escherichia coli DNA binding protein, single-stranded DNA is resistant to both the endo- and exonucleolytic activities of the recBC DNase. Linear duplex DNA, on the other hand, is unwound at a normal rate, but converted to large, single-stranded fragments which are resistant to further hydrolysis. Therefore, in the presence of the binding protein and linear duplex DNA, the recBC enzyme acts not as a DNase, but primarily as an ATP-dependent unwinding enzyme, able to generate large, single-stranded material. Duplex circular DNA containing short, single-stranded gaps is also resistant to the hydrolysis in the presence of the binding protein.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D001426:Bacterial Proteins / Q000502:physiology*; D001665:Binding Sites; D004247:DNA; D003851:Deoxyribonucleases / Q000037:antagonists & inhibitors*; D004926:Escherichia coli / Q000201:enzymology*; D011485:Protein Binding
D001426:Bacterial Proteins; D000255:Adenosine Triphosphate; D004247:DNA; D003851:Deoxyribonucleases