Abstract
Topoisomerases I and II (topo I and topo II) are nuclear enzymes functioning to resolve DNA topological problems during replication, transcription, and other DNA processes. We tested the effects of camptothecin and VP16, specific inhibitors of topo I and II, respectively, on the DNA replication of parvoviruses LuIII and H-1 and found that viral DNA synthesis was suppressed by camptothecin but not by VP16. Transcription of H-1 virus was measured by a nuclear runoff assay and showed no inhibition by camptothecin. Interestingly, topo I in the LuIII virus-infected cell nuclear extract appears to have more activity for covalently binding to viral DNA than that in mock-infected cell nuclear extracts. Our data suggested that this activity was not due to an increased transcription of the topo I gene or to greater amounts of topo I.
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- Avemann K., Knippers R., Koller T., Sogo J. M. Camptothecin, a specific inhibitor of type I DNA topoisomerase, induces DNA breakage at replication forks. Mol Cell Biol. 1988 Aug;8(8):3026–3034. doi: 10.1128/mcb.8.8.3026. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Becker Y., Olshevsky U. Inhibition of Herpes simplex virus replication by camptothecin. Isr J Med Sci. 1973 Nov-Dec;9(11):1578–1581. [PubMed] [Google Scholar]
- Champoux J. J. Topoisomerase I is preferentially associated with isolated replicating simian virus 40 molecules after treatment of infected cells with camptothecin. J Virol. 1988 Oct;62(10):3675–3683. doi: 10.1128/jvi.62.10.3675-3683.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Coderoni S., Paparelli M., Gianfranceschi G. L. Role of calf thymus DNA-topoisomerase I phosphorylation on relaxation activity expression and on DNA-protein interaction. Role of DNA-topoisomerase I phosphorylation. Mol Biol Rep. 1990 Feb;14(1):35–39. doi: 10.1007/BF00422713. [DOI] [PubMed] [Google Scholar]
- Cotmore S. F., Tattersall P. The autonomously replicating parvoviruses of vertebrates. Adv Virus Res. 1987;33:91–174. doi: 10.1016/s0065-3527(08)60317-6. [DOI] [PubMed] [Google Scholar]
- Cozzarelli N. R. DNA gyrase and the supercoiling of DNA. Science. 1980 Feb 29;207(4434):953–960. doi: 10.1126/science.6243420. [DOI] [PubMed] [Google Scholar]
- D'Arpa P., Liu L. F. Topoisomerase-targeting antitumor drugs. Biochim Biophys Acta. 1989 Dec 17;989(2):163–177. doi: 10.1016/0304-419x(89)90041-3. [DOI] [PubMed] [Google Scholar]
- D'Arpa P., Machlin P. S., Ratrie H., 3rd, Rothfield N. F., Cleveland D. W., Earnshaw W. C. cDNA cloning of human DNA topoisomerase I: catalytic activity of a 67.7-kDa carboxyl-terminal fragment. Proc Natl Acad Sci U S A. 1988 Apr;85(8):2543–2547. doi: 10.1073/pnas.85.8.2543. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Diffoot N., Shull B. C., Chen K. C., Stout E. R., Lederman M., Bates R. C. Identical ends are not required for the equal encapsidation of plus- and minus-strand parvovirus LuIII DNA. J Virol. 1989 Jul;63(7):3180–3184. doi: 10.1128/jvi.63.7.3180-3184.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Feinberg A. P., Vogelstein B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem. 1983 Jul 1;132(1):6–13. doi: 10.1016/0003-2697(83)90418-9. [DOI] [PubMed] [Google Scholar]
- Gellert M. DNA topoisomerases. Annu Rev Biochem. 1981;50:879–910. doi: 10.1146/annurev.bi.50.070181.004311. [DOI] [PubMed] [Google Scholar]
- Groudine M., Peretz M., Weintraub H. Transcriptional regulation of hemoglobin switching in chicken embryos. Mol Cell Biol. 1981 Mar;1(3):281–288. doi: 10.1128/mcb.1.3.281. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kreuzer K. N. DNA topoisomerases as potential targets of antiviral action. Pharmacol Ther. 1989;43(3):377–395. doi: 10.1016/0163-7258(89)90017-x. [DOI] [PubMed] [Google Scholar]
- Laskey R. A., Mills A. D. Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. Eur J Biochem. 1975 Aug 15;56(2):335–341. doi: 10.1111/j.1432-1033.1975.tb02238.x. [DOI] [PubMed] [Google Scholar]
- Liu L. F. DNA topoisomerases--enzymes that catalyse the breaking and rejoining of DNA. CRC Crit Rev Biochem. 1983;15(1):1–24. doi: 10.3109/10409238309102799. [DOI] [PubMed] [Google Scholar]
- Osheroff N. Biochemical basis for the interactions of type I and type II topoisomerases with DNA. Pharmacol Ther. 1989;41(1-2):223–241. doi: 10.1016/0163-7258(89)90108-3. [DOI] [PubMed] [Google Scholar]
- Rainwater R., Mann K. Differential increase in topoisomerase II in simian virus 40-infected cells. J Virol. 1990 Feb;64(2):918–921. doi: 10.1128/jvi.64.2.918-921.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rhode S. L., 3rd Construction of a genetic switch for inducible trans-activation of gene expression in eucaryotic cells. J Virol. 1987 May;61(5):1448–1456. doi: 10.1128/jvi.61.5.1448-1456.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rhode S. L., 3rd, Richard S. M. Characterization of the trans-activation-responsive element of the parvovirus H-1 P38 promoter. J Virol. 1987 Sep;61(9):2807–2815. doi: 10.1128/jvi.61.9.2807-2815.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schaack J., Schedl P., Shenk T. Topoisomerase I and II cleavage of adenovirus DNA in vivo: both topoisomerase activities appear to be required for adenovirus DNA replication. J Virol. 1990 Jan;64(1):78–85. doi: 10.1128/jvi.64.1.78-85.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schaak J., Schedl P., Shenk T. Transcription of adenovirus and HeLa cell genes in the presence of drugs that inhibit topoisomerase I and II function. Nucleic Acids Res. 1990 Mar 25;18(6):1499–1508. doi: 10.1093/nar/18.6.1499. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shapiro D. J., Sharp P. A., Wahli W. W., Keller M. J. A high-efficiency HeLa cell nuclear transcription extract. DNA. 1988 Jan-Feb;7(1):47–55. doi: 10.1089/dna.1988.7.47. [DOI] [PubMed] [Google Scholar]
- Shin C. G., Snapka R. M. Exposure to camptothecin breaks leading and lagging strand simian virus 40 DNA replication forks. Biochem Biophys Res Commun. 1990 Apr 16;168(1):135–140. doi: 10.1016/0006-291x(90)91684-k. [DOI] [PubMed] [Google Scholar]
- Snapka R. M., Powelson M. A., Strayer J. M. Swiveling and decatenation of replicating simian virus 40 genomes in vivo. Mol Cell Biol. 1988 Feb;8(2):515–521. doi: 10.1128/mcb.8.2.515. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Snapka R. M. Topoisomerase inhibitors can selectively interfere with different stages of simian virus 40 DNA replication. Mol Cell Biol. 1986 Dec;6(12):4221–4227. doi: 10.1128/mcb.6.12.4221. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sutcliffe J. A., Gootz T. D., Barrett J. F. Biochemical characteristics and physiological significance of major DNA topoisomerases. Antimicrob Agents Chemother. 1989 Dec;33(12):2027–2033. doi: 10.1128/aac.33.12.2027. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wang J. C. DNA topoisomerases. Annu Rev Biochem. 1985;54:665–697. doi: 10.1146/annurev.bi.54.070185.003313. [DOI] [PubMed] [Google Scholar]
- Wong M. L., Hsu M. T. Involvement of topoisomerases in replication, transcription, and packaging of the linear adenovirus genome. J Virol. 1990 Feb;64(2):691–699. doi: 10.1128/jvi.64.2.691-699.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yang L., Wold M. S., Li J. J., Kelly T. J., Liu L. F. Roles of DNA topoisomerases in simian virus 40 DNA replication in vitro. Proc Natl Acad Sci U S A. 1987 Feb;84(4):950–954. doi: 10.1073/pnas.84.4.950. [DOI] [PMC free article] [PubMed] [Google Scholar]




