This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Francke, B Articles by Hay, J Search for Related Content PubMed PubMed Citation Articles by Francke, B Articles by Hay, J

Alkaline DNase activity in cells infected with a temperature-sensitive mutant of herpes simplex virus type 2.

ABSTRACT

BHK cells infected with the temperature-sensitive mutant ts13 of herpes simplex virus type 2 at a nonpermissive temperature lack the alkaline nuclease activity, which is induced by the mutant at a permissive temperature and by wild-type virus at either temperature. For ts13, enzyme activity could be induced by a temperature shift to permissive conditions, but not in the presence of cycloheximide. After a shift from permissive to nonpermissive conditions in the presence of cycloheximide, the activity was stable in wild-type, but not in mutant-infected, cells. After extensive purification, the wild-type nuclease was fourfold more heat stable in the presence of substrate than was the mutant enzyme. Mixtures of both purified enzymes showed the predicted intermediate stabilities. The results strongly suggest that the enzyme is virus coded and that the mutant possesses a lesion in the structural gene of the enzyme.

This article has been cited by other articles:

• Mikhailov, V. S., Okano, K., Rohrmann, G. F. (2004). Specificity of the Endonuclease Activity of the Baculovirus Alkaline Nuclease for Single-stranded DNA. J. Biol. Chem. 279: 14734-14745 [Abstract] [Full Text]  
• Mikhailov, V. S., Okano, K., Rohrmann, G. F. (2003). Baculovirus Alkaline Nuclease Possesses a 5'->3' Exonuclease Activity and Associates with the DNA-Binding Protein LEF-3. J. Virol. 77: 2436-2444 [Abstract] [Full Text]