Skip to main content
PMC home page
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1979 Aug 24;6(12):3717–3731. doi: 10.1093/nar/6.12.3717

Nuclease activity associated with the Ustilago maydis virus induced killer proteins.

R Levine, Y Koltin, J Kandel
PMCID: PMC327973  PMID: 493119

Abstract

An in vitro nuclease activity was found to be associated with the purified killer proteins of Ustilago maydis. The proteins are effective against single stranded RNA, single and double stranded DNA. Endonucleolytic activity was confirmed by cleavage of circular molecules of 0x174 and PM2. Double stranded RNA did not appear to serve as a substrate.

Full text

PDF
3717

Images in this article

3720Image
on p.3720
3726Image
on p.3726
3727Image
on p.3727
3728Image
on p.3728

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Beerman T. A., Lebowitz J. Further analysis of the altered secondary structure of superhelical DNA. Sensitivity to methylmercuric hydroxide a chemical probe for unpaired bases. J Mol Biol. 1973 Sep 25;79(3):451–470. doi: 10.1016/0022-2836(73)90398-7. [DOI] [PubMed] [Google Scholar]
  2. Brack C., Bickle T. A., Yuan R. The relation of single-stranded regions in bacteriophage PM2 supercoiled DNA to the early melting sequences. J Mol Biol. 1975 Aug 25;96(4):693–702. doi: 10.1016/0022-2836(75)90146-1. [DOI] [PubMed] [Google Scholar]
  3. Espejo R. T., Canelo E. S., Sinsheimer R. L. Replication of bacteriophage PM2 deoxyribonucleic acid: a closed circular double-stranded molecule. J Mol Biol. 1971 Mar 28;56(3):597–621. doi: 10.1016/0022-2836(71)90404-9. [DOI] [PubMed] [Google Scholar]
  4. Henderson D. R., Joklik W. K. The mechanism of interferon induction by UV-irradiated reovirus. Virology. 1978 Dec;91(2):389–406. doi: 10.1016/0042-6822(78)90386-0. [DOI] [PubMed] [Google Scholar]
  5. Hollings M. Mycoviruses: viruses that infect fungi. Adv Virus Res. 1978;22:1–53. doi: 10.1016/s0065-3527(08)60771-x. [DOI] [PubMed] [Google Scholar]
  6. Koltin Y., Day P. R. Inheritance of killer phenotypes and double-stranded RNA in Ustilago maydis. Proc Natl Acad Sci U S A. 1976 Feb;73(2):594–598. doi: 10.1073/pnas.73.2.594. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Koltin Y., Day P. R. Specificity of Ustilago maydis killer proteins. Appl Microbiol. 1975 Oct;30(4):694–696. doi: 10.1128/am.30.4.694-696.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Koltin Y., Kandel J. S. Killer Phenomenon in USTILAGO MAYDIS: The Organization of the Viral Genome. Genetics. 1978 Feb;88(2):267–276. doi: 10.1093/genetics/88.2.267. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Koltin Y., Mayer I., Steinlauf R. Killer phenomenon in Ustilago maydis: mapping viral functions. Mol Gen Genet. 1978 Oct 30;166(2):181–186. doi: 10.1007/BF00285920. [DOI] [PubMed] [Google Scholar]
  10. Koltin Y. Virus-like particles in Ustilago maydis: mutants with partial genomes. Genetics. 1977 Jul;86(3):527–534. doi: 10.1093/genetics/86.3.527. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. Lemke P. A. Viruses of eucaryotic microorganisms. Annu Rev Microbiol. 1976;30:105–145. doi: 10.1146/annurev.mi.30.100176.000541. [DOI] [PubMed] [Google Scholar]
  13. Moore K. H., Johnson P. H., Chandler S. E., Grossman L. I. A restriction endonuclease cleavage map of mouse mitochondrial DNA. Nucleic Acids Res. 1977;4(5):1273–1289. doi: 10.1093/nar/4.5.1273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Pelham H. R., Jackson R. J. An efficient mRNA-dependent translation system from reticulocyte lysates. Eur J Biochem. 1976 Aug 1;67(1):247–256. doi: 10.1111/j.1432-1033.1976.tb10656.x. [DOI] [PubMed] [Google Scholar]
  15. Puhalla J. E. Compatibility reactions on solid medium and interstrain inhibition in Ustilago maydis. Genetics. 1968 Nov;60(3):461–474. doi: 10.1093/genetics/60.3.461. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Razin A., Sedat J. W., Sinsheimer R. L. Structure of the DNA of bacteriophage phiX174. VII. Methylation. J Mol Biol. 1970 Oct 28;53(2):251–259. doi: 10.1016/0022-2836(70)90298-6. [DOI] [PubMed] [Google Scholar]
  17. Sharp P. A., Sugden B., Sambrook J. Detection of two restriction endonuclease activities in Haemophilus parainfluenzae using analytical agarose--ethidium bromide electrophoresis. Biochemistry. 1973 Jul 31;12(16):3055–3063. doi: 10.1021/bi00740a018. [DOI] [PubMed] [Google Scholar]
  18. Shatkin A. J., Sipe J. D., Loh P. Separation of ten reovirus genome segments by polyacrylamide gel electrophoresis. J Virol. 1968 Oct;2(10):986–991. doi: 10.1128/jvi.2.10.986-991.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Wang D., Moore S. Polyspermine-ribonuclease prepared by cross-linkage with dimethyl suberimidate. Biochemistry. 1977 Jun 28;16(13):2937–2942. doi: 10.1021/bi00632a021. [DOI] [PubMed] [Google Scholar]
  20. Wang J. C. Interactions between twisted DNAs and enzymes: the effects of superhelical turns. J Mol Biol. 1974 Aug 25;87(4):797–816. doi: 10.1016/0022-2836(74)90085-0. [DOI] [PubMed] [Google Scholar]
  21. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  22. Wreschner D., Melloul D., Herzberg M. Interaction between membrane functions and protein synthesis in reticulocytes: specific cleavage of 28-S ribosomal RNA by a membrane constituent. Eur J Biochem. 1978 Apr;85(1):233–240. doi: 10.1111/j.1432-1033.1978.tb12231.x. [DOI] [PubMed] [Google Scholar]
  23. Wrigley C. W. Analytical fractionation of plant and animal proteins by gel electrofocusing. J Chromatogr. 1968 Aug 27;36(3):362–365. doi: 10.1016/s0021-9673(01)92959-0. [DOI] [PubMed] [Google Scholar]
  24. Young T. W., Yagiu M. A comparison of the killer character in different yeasts and its classification. Antonie Van Leeuwenhoek. 1978;44(1):59–77. doi: 10.1007/BF00400077. [DOI] [PubMed] [Google Scholar]
  25. de Graaf F. K., Stukart M. J., Boogerd F. C., Metselaar K. Limited proteolysis of cloacin DF13 and characterization of the cleavage products. Biochemistry. 1978 Mar 21;17(6):1137–1142. doi: 10.1021/bi00599a031. [DOI] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES