DNase inhibition by the adenovirus DNA-binding protein exhibits specificity for the enzyme but not for the secondary structure of the DNA.
The adenovirus-specific DNA-binding protein (DBP) has been shown to inhibit the hydrolysis of single-stranded DNA by a DNase isolated from KB cells, (Nass, K., and Frenkel, G.D. (1980). J. Virol. 35, 314-319). The specificity of the inhibition has now been investigated. The DBP inhibits the hydrolysis of single-stranded DNA by several different DNases (DNase II, KB DNase, S1 nuclease) under a variety of reaction conditions, but it has no effect on DNase I-catalyzed hydrolysis of single-stranded DNA. The DBP also inhibits the rate of hydrolysis of double-stranded DNA by KB DNase and DNase II, but has no effect on DNase I-catalyzed hydrolysis of this substrate. The DBP also inhibits the dephosphorylation of 5'-phosphoryl-terminated DNA by bacterial alkaline phosphatase but stimulates the phosphorylation of 5'-hydroxyl-terminated DNA by polynucleotide kinase.
D000256:Adenoviridae / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D004265:DNA Helicases / Q000494:pharmacology*; D004279:DNA, Viral / Q000378:metabolism*; D004268:DNA-Binding Proteins; D003851:Deoxyribonucleases / Q000037:antagonists & inhibitors*; D006868:Hydrolysis; D010766:Phosphorylation; D014764:Viral Proteins / Q000494:pharmacology*
D004279:DNA, Viral; D004268:DNA-Binding Proteins; D014764:Viral Proteins; D003851:Deoxyribonucleases; D004265:DNA Helicases