Skip to main content
NCBI home page
Journal of Virology logoLink to Journal of Virology
. 1990 Jul;64(7):3545–3550. doi: 10.1128/jvi.64.7.3545-3550.1990

Sequence and functional differences between Schmidt-Ruppin D and Schmidt-Ruppin A strains of pp60v-src.

S Reddy 1, D Mazzu 1, D Mahan 1, D Shalloway 1
PMCID: PMC249629  PMID: 2161957

Abstract

We show that Schmidt-Ruppin D pp60v-src kinase activity is reduced by a mutation previously shown to be associated with Schmidt-Ruppin A pp60v-src temperature sensitivity and that its reduced transforming activity is associated with a conformational change in the SH3 region. The evolutionary relationship of seven v-src strains was studied by using parsimony analysis.

Full text

PDF
3545

Images in this article

3548Image
on p.3548

Selected References

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

  1. Cross F. R., Garber E. A., Hanafusa H. N-terminal deletions in Rous sarcoma virus p60src: effects on tyrosine kinase and biological activities and on recombination in tissue culture with the cellular src gene. Mol Cell Biol. 1985 Oct;5(10):2789–2795. doi: 10.1128/mcb.5.10.2789. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Czernilofsky A. P., Levinson A. D., Varmus H. E., Bishop J. M., Tischer E., Goodman H. Corrections to the nucleotide sequence of the src gene of Rous sarcoma virus. Nature. 1983 Feb 24;301(5902):736–738. doi: 10.1038/301736b0. [DOI] [PubMed] [Google Scholar]
  3. Dougherty J. P., Temin H. M. High mutation rate of a spleen necrosis virus-based retrovirus vector. Mol Cell Biol. 1986 Dec;6(12):4387–4395. doi: 10.1128/mcb.6.12.4387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fincham V. J., Wyke J. A. Localization of temperature-sensitive transformation mutations and back mutations in the Rous sarcoma virus src gene. J Virol. 1986 May;58(2):694–699. doi: 10.1128/jvi.58.2.694-699.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Garber E. A., Mayer B. J., Jove R., Hanafusa H. Analysis of p60v-src mutants carrying lesions involved in temperature sensitivity. J Virol. 1987 Feb;61(2):354–360. doi: 10.1128/jvi.61.2.354-360.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hagino-Yamagishi K., Ikawa S., Kawai S., Hihara H., Yamamoto T., Toyoshima K. Characterization of two strains of avian sarcoma virus isolated from avian lymphatic leukosis virus-induced sarcomas. Virology. 1984 Sep;137(2):266–275. doi: 10.1016/0042-6822(84)90218-6. [DOI] [PubMed] [Google Scholar]
  7. Hanks S. K., Quinn A. M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science. 1988 Jul 1;241(4861):42–52. doi: 10.1126/science.3291115. [DOI] [PubMed] [Google Scholar]
  8. Hirai H., Varmus H. E. Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src. Mol Cell Biol. 1990 Apr;10(4):1307–1318. doi: 10.1128/mcb.10.4.1307. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Johnson P. J., Coussens P. M., Danko A. V., Shalloway D. Overexpressed pp60c-src can induce focus formation without complete transformation of NIH 3T3 cells. Mol Cell Biol. 1985 May;5(5):1073–1083. doi: 10.1128/mcb.5.5.1073. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Jove R., Hanafusa H. Cell transformation by the viral src oncogene. Annu Rev Cell Biol. 1987;3:31–56. doi: 10.1146/annurev.cb.03.110187.000335. [DOI] [PubMed] [Google Scholar]
  11. KLEMENT V., SVOBODA J. Induction of tumours in Syrian hamsters by two variants of Rous sarcoma virus. Folia Biol (Praha) 1963 Jun;9:181–188. [PubMed] [Google Scholar]
  12. Kato J. Y., Takeya T., Grandori C., Iba H., Levy J. B., Hanafusa H. Amino acid substitutions sufficient to convert the nontransforming p60c-src protein to a transforming protein. Mol Cell Biol. 1986 Dec;6(12):4155–4160. doi: 10.1128/mcb.6.12.4155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kmiecik T. E., Shalloway D. Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell. 1987 Apr 10;49(1):65–73. doi: 10.1016/0092-8674(87)90756-2. [DOI] [PubMed] [Google Scholar]
  14. Koch C. A., Moran M., Sadowski I., Pawson T. The common src homology region 2 domain of cytoplasmic signaling proteins is a positive effector of v-fps tyrosine kinase function. Mol Cell Biol. 1989 Oct;9(10):4131–4140. doi: 10.1128/mcb.9.10.4131. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Levy J. B., Iba H., Hanafusa H. Activation of the transforming potential of p60c-src by a single amino acid change. Proc Natl Acad Sci U S A. 1986 Jun;83(12):4228–4232. doi: 10.1073/pnas.83.12.4228. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Lipsich L. A., Lewis A. J., Brugge J. S. Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses. J Virol. 1983 Nov;48(2):352–360. doi: 10.1128/jvi.48.2.352-360.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  18. Mayer B. J., Jove R., Krane J. F., Poirier F., Calothy G., Hanafusa H. Genetic lesions involved in temperature sensitivity of the src gene products of four Rous sarcoma virus mutants. J Virol. 1986 Dec;60(3):858–867. doi: 10.1128/jvi.60.3.858-867.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Nishizawa M., Mayer B. J., Takeya T., Yamamoto T., Toyoshima K., Hanafusa H., Kawai S. Two independent mutations are required for temperature-sensitive cell transformation by a Rous sarcoma virus temperature-sensitive mutant. J Virol. 1985 Dec;56(3):743–749. doi: 10.1128/jvi.56.3.743-749.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Parsons J. T., Weber M. J. Genetics of src: structure and functional organization of a protein tyrosine kinase. Curr Top Microbiol Immunol. 1989;147:79–127. doi: 10.1007/978-3-642-74697-0_3. [DOI] [PubMed] [Google Scholar]
  21. Parsons S. J., McCarley D. J., Ely C. M., Benjamin D. C., Parsons J. T. Monoclonal antibodies to Rous sarcoma virus pp60src react with enzymatically active cellular pp60src of avian and mammalian origin. J Virol. 1984 Aug;51(2):272–282. doi: 10.1128/jvi.51.2.272-282.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Pawson T. Non-catalytic domains of cytoplasmic protein-tyrosine kinases: regulatory elements in signal transduction. Oncogene. 1988 Nov;3(5):491–495. [PubMed] [Google Scholar]
  23. Raymond V. W., Parsons J. T. Identification of an amino terminal domain required for the transforming activity of the Rous sarcoma virus src protein. Virology. 1987 Oct;160(2):400–410. doi: 10.1016/0042-6822(87)90011-0. [DOI] [PubMed] [Google Scholar]
  24. Reddy S., Yaciuk P., Kmiecik T. E., Coussens P. M., Shalloway D. v-src mutations outside the carboxyl-coding region are not sufficient to fully activate transformation by pp60c-src in NIH 3T3 cells. Mol Cell Biol. 1988 Feb;8(2):704–712. doi: 10.1128/mcb.8.2.704. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. SCHMIDT-RUPPIN K. H. HETEROTRANSPLANTATION OF ROUS SARCOMA AND ROUS SARCOMA VIRUS TO MAMMALS. Oncology. 1964;17:247–272. doi: 10.1159/000224235. [DOI] [PubMed] [Google Scholar]
  26. Schwartz D. E., Tizard R., Gilbert W. Nucleotide sequence of Rous sarcoma virus. Cell. 1983 Mar;32(3):853–869. doi: 10.1016/0092-8674(83)90071-5. [DOI] [PubMed] [Google Scholar]
  27. Shalloway D., Zelenetz A. D., Cooper G. M. Molecular cloning and characterization of the chicken gene homologous to the transforming gene of Rous sarcoma virus. Cell. 1981 May;24(2):531–541. doi: 10.1016/0092-8674(81)90344-5. [DOI] [PubMed] [Google Scholar]
  28. Southern P. J., Berg P. Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter. J Mol Appl Genet. 1982;1(4):327–341. [PubMed] [Google Scholar]
  29. Takeya T., Hanafusa H. DNA sequence of the viral and cellular src gene of chickens. II. Comparison of the src genes of two strains of avian sarcoma virus and of the cellular homolog. J Virol. 1982 Oct;44(1):12–18. doi: 10.1128/jvi.44.1.12-18.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Takeya T., Hanafusa H. Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus. Cell. 1983 Mar;32(3):881–890. doi: 10.1016/0092-8674(83)90073-9. [DOI] [PubMed] [Google Scholar]
  31. Verderame M. F., Kaplan J. M., Varmus H. E. A mutation in v-src that removes a single conserved residue in the SH-2 domain of pp60v-src restricts transformation in a host-dependent manner. J Virol. 1989 Jan;63(1):338–348. doi: 10.1128/jvi.63.1.338-348.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Wang L. H., Hanafusa H. Avian sarcoma viruses. Virus Res. 1988 Feb;9(2-3):159–203. doi: 10.1016/0168-1702(88)90030-5. [DOI] [PubMed] [Google Scholar]
  33. Yaciuk P., Shalloway D. Features of the pp60v-src carboxyl terminus that are required for transformation. Mol Cell Biol. 1986 Aug;6(8):2807–2819. doi: 10.1128/mcb.6.8.2807. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES