Skip to main content
NCBI home page
Journal of Virology logoLink to Journal of Virology
. 1974 Feb;13(2):305–311. doi: 10.1128/jvi.13.2.305-311.1974

Histones Stimulate Polyribonucleotide-Directed Polydeoxyribonucleotide Synthesis by Murine Leukemia Virus

Kenneth F Manly 1
PMCID: PMC355298  PMID: 4855739

Abstract

The rate of homoribopolymer-directed DNA synthesis by detergent-disrupted Moloney murine leukemia virus can be stimulated or inhibited by histone, depending on the ratio of histone to template. Of the fractions which can be separated from the whole histone, f1 causes both the greatest stimulation and the greatest inhibition. The effect of histone f1 is qualitatively similar whether the template is polyadenylate (poly A), polycytidylate, or polyuridylate, but the stimulation is greatest with poly A. The pattern of stimulation and inhibition differs, however, for a different polymerase; the DNA polymerase of Micrococcus luteus is inhibited by histone concentrations which stimulate the viral enzyme and stimulated by concentrations which inhibit the viral enzyme. For the viral enzyme, the optimum histone concentration is unaffected by changes in the virus or primer concentration; but it varies in proportion to the template concentration, suggesting that histone acts by combining stoichiometrically with the template. These data raise the possibility that a histone-like protein may participate in the synthesis of the provirus of RNA tumor viruses.

Full text

PDF
305

Selected References

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

  1. Baltimore D. RNA-dependent DNA polymerase in virions of RNA tumour viruses. Nature. 1970 Jun 27;226(5252):1209–1211. doi: 10.1038/2261209a0. [DOI] [PubMed] [Google Scholar]
  2. Baltimore D., Smoler D. Primer requirement and template specificity of the DNA polymerase of RNA tumor viruses. Proc Natl Acad Sci U S A. 1971 Jul;68(7):1507–1511. doi: 10.1073/pnas.68.7.1507. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Davis N. L., Rueckert R. R. Properties of a ribonucleoprotein particle isolated from Nonidet P-40-treated Rous sarcoma virus. J Virol. 1972 Nov;10(5):1010–1020. doi: 10.1128/jvi.10.5.1010-1020.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fleissner E. Chromatographic separation and antigenic analysis of proteins of the oncornaviruses. I. Avian leukemia-sarcoma viruses. J Virol. 1971 Nov;8(5):778–785. doi: 10.1128/jvi.8.5.778-785.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Huberman J. A., Kornberg A., Alberts B. M. Stimulation of T4 bacteriophage DNA polymerase by the protein product of T4 gene 32. J Mol Biol. 1971 Nov 28;62(1):39–52. doi: 10.1016/0022-2836(71)90129-x. [DOI] [PubMed] [Google Scholar]
  6. Hurwitz J., Leis J. P. RNA-dependent DNA polymerase activity of RNA tumor viruses. I. Directing influence of DNA in the reaction. J Virol. 1972 Jan;9(1):116–129. doi: 10.1128/jvi.9.1.116-129.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Johns E. W. A method for the selective extraction of histone fractions f2(a)1 and f2(a)2 from calf thymus deoxyribonucleoprotein at pH7. Biochem J. 1967 Nov;105(2):611–614. doi: 10.1042/bj1050611. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Johns E. W. Studies on histones. 7. Preparative methods for histone fractions from calf thymus. Biochem J. 1964 Jul;92(1):55–59. doi: 10.1042/bj0920055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Johns E. W. The electrophoresis of histones in polyacrylamide gel and their quantitative determination. Biochem J. 1967 Jul;104(1):78–82. doi: 10.1042/bj1040078. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kacian D. L., Watson K. F., Burny A., Spiegelman S. Purification of the DNA polymerase of avian myeloblastosis virus. Biochim Biophys Acta. 1971 Sep 24;246(3):365–383. doi: 10.1016/0005-2787(71)90773-8. [DOI] [PubMed] [Google Scholar]
  11. Kuo C. H., August J. T. Histone or bacterial basic protein required for replication of bacteriophage RNA. Nat New Biol. 1972 May 24;237(73):105–108. doi: 10.1038/newbio237105a0. [DOI] [PubMed] [Google Scholar]
  12. 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]
  13. Leis J. P., Hurwitz J. Isolation and characterization of a protein that stimulates DNA synthesis from avian myeloblastosis virus. Proc Natl Acad Sci U S A. 1972 Aug;69(8):2331–2335. doi: 10.1073/pnas.69.8.2331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Reuben R. C., Gefter M. L. A DNA-binding protein induced by bacteriophage T7. Proc Natl Acad Sci U S A. 1973 Jun;70(6):1846–1850. doi: 10.1073/pnas.70.6.1846. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Sigal N., Delius H., Kornberg T., Gefter M. L., Alberts B. A DNA-unwinding protein isolated from Escherichia coli: its interaction with DNA and with DNA polymerases. Proc Natl Acad Sci U S A. 1972 Dec;69(12):3537–3541. doi: 10.1073/pnas.69.12.3537. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Stavis R. L., August J. T. The biochemistry of RNA bacteriophage replication. Annu Rev Biochem. 1970;39:527–560. doi: 10.1146/annurev.bi.39.070170.002523. [DOI] [PubMed] [Google Scholar]
  17. Temin H. M., Baltimore D. RNA-directed DNA synthesis and RNA tumor viruses. Adv Virus Res. 1972;17:129–186. doi: 10.1016/s0065-3527(08)60749-6. [DOI] [PubMed] [Google Scholar]
  18. Temin H. M., Mizutani S. RNA-dependent DNA polymerase in virions of Rous sarcoma virus. Nature. 1970 Jun 27;226(5252):1211–1213. doi: 10.1038/2261211a0. [DOI] [PubMed] [Google Scholar]
  19. WILKINSON G. N. Statistical estimations in enzyme kinetics. Biochem J. 1961 Aug;80:324–332. doi: 10.1042/bj0800324. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wickner W., Schekman R., Geider K., Kornberg A. A new form of DNA polymerase 3 and a copolymerase replicate a long, single-stranded primer-template. Proc Natl Acad Sci U S A. 1973 Jun;70(6):1764–1767. doi: 10.1073/pnas.70.6.1764. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Wright B. S., O'Brien P. A., Shibley G. P., Mayyasi S. A., Lasfargues J. C. Infection of an established mouse bone marrow cell line (JLS-V9) with Rauscher and Moloney murine leukemia viruses. Cancer Res. 1967 Sep;27(9):1672–1677. [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES