DNase inhibition by the adenovirus DNA-binding protein exhibits specificity for the enzyme but not for the secondary structure of the DNA

Gerald D. Frenkel, Kathleen Horan

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)443-448
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume110
Issue number2
DOIs
StatePublished - Jan 27 1983
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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