Skip to main content
NCBI home page
Journal of Virology logoLink to Journal of Virology
. 1970 Oct;6(4):445–454. doi: 10.1128/jvi.6.4.445-454.1970

Isolation and Characterization of Two Basic Internal Proteins from the T-Even Bacteriophages 1

Kenneth R Stone 1, Donald J Cummings 1
PMCID: PMC376142  PMID: 5497890

Abstract

Two species of basic internal proteins were found in osmotic shock supernatant solutions of bacteriophages T4B, T4D, T2H, T2L, and T6. The major species of protein isolated had a molecular weight of approximately 21,000 daltons, whereas the minor protein molecular weight was near 9,500 daltons. The two protein species exhibited unique isoelectric points and amino acid compositions. The 21,000-dalton protein of T2L showed major electrophoretic and compositional differences from the other 21,000-dalton proteins isolated. Similarities between the 21,000-dalton proteins and phage lysozyme are discussed.

Full text

PDF
445

Images in this article

450Image
on p.450

Selected References

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

  1. AMES B. N., DUBIN D. T., ROSENTHAL S. M. Presence of polyamines in certain bacterial viruses. Science. 1958 Apr 11;127(3302):814–815. doi: 10.1126/science.127.3302.814-a. [DOI] [PubMed] [Google Scholar]
  2. Anderson T. F. The Activation of the Bacterial Virus T4 by l-Tryptophan. J Bacteriol. 1948 May;55(5):637–649. doi: 10.1128/jb.55.5.637-649.1948. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bachrach U., Friedmann A. Purification and some possible functions of internal proteins from coliphage T2. Biochem Biophys Res Commun. 1967 Mar 9;26(5):596–601. doi: 10.1016/0006-291x(67)90107-6. [DOI] [PubMed] [Google Scholar]
  4. Bachrach U., Levin R., Friedmann A. Studies on phage internal proteins: isolation of protein-DNA complexes from T2 phages and from phage-infected bacteria. Virology. 1970 Apr;40(4):882–892. doi: 10.1016/0042-6822(70)90134-0. [DOI] [PubMed] [Google Scholar]
  5. Bishop D. H., Claybrook J. R., Spiegelman S. Electrophoretic separation of viral nucleic acids on polyacrylamide gels. J Mol Biol. 1967 Jun 28;26(3):373–387. doi: 10.1016/0022-2836(67)90310-5. [DOI] [PubMed] [Google Scholar]
  6. CHAPRONIERE-RICKENBERG D. M., MAHLER H. R., FRASER D. THE INTERACTION OF DNA AND INTERNAL PROTEIN FROM COLIPHAGE T2. Virology. 1964 May;23:96–102. doi: 10.1016/s0042-6822(64)80012-x. [DOI] [PubMed] [Google Scholar]
  7. CUMMINGS D. J. Subunit basis of head configurational changes in T2 bacteriophage. Biochim Biophys Acta. 1963 Mar 26;68:472–480. doi: 10.1016/0006-3002(63)90169-0. [DOI] [PubMed] [Google Scholar]
  8. Cummings D. J., Chapman V. A., DeLong S. S., Kusy A. R., Stone K. R. Characterization of T-even bacteriophage substructures. II. Tail plates. J Virol. 1970 Oct;6(4):545–555. doi: 10.1128/jvi.6.4.545-555.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Cummings D. J., Kusy A. R., Chapman V. A., DeLong S. S., Stone K. R. Characterization of T-even bacteriophage substructures. I. Tail fibers and tail tubes. J Virol. 1970 Oct;6(4):534–544. doi: 10.1128/jvi.6.4.534-544.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Dale G., Latner A. L. Isoelectric focusing in polyacrylamide gels. Lancet. 1968 Apr 20;1(7547):847–848. doi: 10.1016/s0140-6736(68)90303-6. [DOI] [PubMed] [Google Scholar]
  11. Davison P. F. Proteins in denaturing solvents: gel exclusion studies. Science. 1968 Aug 30;161(3844):906–907. doi: 10.1126/science.161.3844.906. [DOI] [PubMed] [Google Scholar]
  12. Duckworth D. H. The metabolism of T4 phage ghost-infected cells. I. Macromolecular synthesis and ransport of nucleic acid and protein precursors. Virology. 1970 Mar;40(3):673–684. doi: 10.1016/0042-6822(70)90212-6. [DOI] [PubMed] [Google Scholar]
  13. Eddleman H. L., Champe S. P. Components in T4-infected cells associated with phage assembly. Virology. 1966 Nov;30(3):471–481. doi: 10.1016/0042-6822(66)90123-1. [DOI] [PubMed] [Google Scholar]
  14. Emrich J. Lysis of T4-infected bacteria in the absence of lysozyme. Virology. 1968 May;35(1):158–165. doi: 10.1016/0042-6822(68)90315-2. [DOI] [PubMed] [Google Scholar]
  15. Emrich J., Streisinger G. The role of phage lysozyme in the life cycle of phage T4. Virology. 1968 Nov;36(3):387–391. doi: 10.1016/0042-6822(68)90163-3. [DOI] [PubMed] [Google Scholar]
  16. Forrest G. L., Cummings D. J. Head proteins from T-even bacteriophage. I. Molecular weight characterization. J Virol. 1970 Mar;5(3):398–405. doi: 10.1128/jvi.5.3.398-405.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. HERRIOTT R. M., BARLOW J. L. The protein coats or ghosts of coliphage T2. I. Preparation, assay, and some chemical properties. J Gen Physiol. 1957 May 20;40(5):809–825. doi: 10.1085/jgp.40.5.809. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. HERSHEY A. D. An upper limit to the protein content of the germinal substance of bacteriophage T2. Virology. 1955 May;1(1):108–127. doi: 10.1016/0042-6822(55)90009-x. [DOI] [PubMed] [Google Scholar]
  19. HERSHEY A. D. Some minor components of bacteriophage T2 particles. Virology. 1957 Oct;4(2):237–264. doi: 10.1016/0042-6822(57)90061-2. [DOI] [PubMed] [Google Scholar]
  20. HIRS C. H. The oxidation of ribonuclease with performic acid. J Biol Chem. 1956 Apr;219(2):611–621. [PubMed] [Google Scholar]
  21. HUPPERT J., PANIJEL J. Recherches sur les prolysines. II. Le cas général de la synthèse des prolysines. Ann Inst Pasteur (Paris) 1956 Jun;90(6):711–727. [PubMed] [Google Scholar]
  22. Inouye M., Tsugita A. Amino acid sequence of T2 phage lysozyme. J Mol Biol. 1968 Oct 14;37(1):213–223. doi: 10.1016/0022-2836(68)90084-3. [DOI] [PubMed] [Google Scholar]
  23. KELLENBERGER E. Vegetative bacteriophage and the maturation of the virus particles. Adv Virus Res. 1961;8:1–61. doi: 10.1016/s0065-3527(08)60682-x. [DOI] [PubMed] [Google Scholar]
  24. KOZLOFF L. M., LUTE M. Calcium content of bacteriophage T2. Biochim Biophys Acta. 1960 Jan 29;37:420–424. doi: 10.1016/0006-3002(60)90497-2. [DOI] [PubMed] [Google Scholar]
  25. Kokurina N. K., Tikhonenko T. I. Vydelenie i fraktsionirovanie vnutrennikh belkov bakteriofagov T2 i DFVI. Vopr Virusol. 1969 Mar-Apr;14(2):224–228. [PubMed] [Google Scholar]
  26. LEVINE L., BARLOW J. L., VAN VUNAKIS H. An internal protein in T2 and T4 bacteriophages. Virology. 1958 Dec;6(3):702–717. doi: 10.1016/0042-6822(58)90116-8. [DOI] [PubMed] [Google Scholar]
  27. MINAGAWA T. Some characteristics of the internal protein phage T2. Virology. 1961 Apr;13:515–527. doi: 10.1016/0042-6822(61)90283-5. [DOI] [PubMed] [Google Scholar]
  28. MURAKAMI W. T., VAN VUNAKIS H., LEVINE L. Synthesis of T2 internal protein in infected Escherichia coli, strain B. Virology. 1959 Dec;9:624–635. doi: 10.1016/0042-6822(59)90153-9. [DOI] [PubMed] [Google Scholar]
  29. McConahey P. J., Dixon F. J. A method of trace iodination of proteins for immunologic studies. Int Arch Allergy Appl Immunol. 1966;29(2):185–189. doi: 10.1159/000229699. [DOI] [PubMed] [Google Scholar]
  30. Nozaki Y., Tanford C. Acid-base titrations in concentrated guanidine hydrochloride. Dissociation constants of the guamidinium ion and of some amino acids. J Am Chem Soc. 1967 Feb 15;89(4):736–742. doi: 10.1021/ja00980a002. [DOI] [PubMed] [Google Scholar]
  31. PANIJEL J., HUPPERT J. Recherches sur les prolysines. I. La prolysine du phage Fcz. Ann Inst Pasteur (Paris) 1956 May;90(5):619–636. [PubMed] [Google Scholar]
  32. PANIJEL J. [The enzymic activities connected with phages and with the phage synthesis]. Ann Inst Pasteur (Paris) 1959 Aug;97:198–217. [PubMed] [Google Scholar]
  33. RHODES M. B., AZARI P. R., FEENEY R. E. Analysis, fractionation, and purification of egg white proteins with cellulose-cation exchanger. J Biol Chem. 1958 Jan;230(1):399–408. [PubMed] [Google Scholar]
  34. Sternberg N., Champe S. P. Genetic determinant of an internal peptide of bacteriophage T4. J Mol Biol. 1969 Dec 28;46(3):377–392. doi: 10.1016/0022-2836(69)90183-1. [DOI] [PubMed] [Google Scholar]
  35. Tsugita A., Inouye M. Complete primary structure of phage lysozyme from Escherichia coli T4. J Mol Biol. 1968 Oct 14;37(1):201–212. doi: 10.1016/0022-2836(68)90083-1. [DOI] [PubMed] [Google Scholar]

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

RESOURCES