1887

Abstract

SUMMARY

Bacteriophage MX-1 is a virulent DNA phage for Myxococcus. The host range includes strains of and . The phage has a sedimentation coefficient ( ) of 1145S and a density of 1.531 g/ml. By using SDS-polyacrylamide gel electrophoresis, 23 phage proteins with apparent mol. wt. between 10000 and 150000 were resolved. Gel filtration in the presence of nonionic detergent partially resolved the proteins. The fraction excluded from Sephadex G-100, fraction 1, contains two glycoproteins. Fraction 1 was resolved into three fractions (1.1, 1.2 and 1.3) by chromatography on Sephadex G-200. The glycoproteins were present in fraction 1.2; all the proteins from this fraction were derived from the phage tail. Comparison of the amino-acid, hexosamine and neutral-sugar compositions of the two glycoproteins showed that they are distinct molecular species; the smaller molecule is not a subunit of the larger. The significance of these findings is discussed and compared with the proteins of the tails of T-even phage of .

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-30-1-99
1976-01-01
2024-04-25
Loading full text...

Full text loading...

/deliver/fulltext/jgv/30/1/JV0300010099.html?itemId=/content/journal/jgv/10.1099/0022-1317-30-1-99&mimeType=html&fmt=ahah

References

  1. Alvarez G., Salas E., Perez N., Celis J. E. 1972; ϕ 29 Bacteriophage structural proteins. Journal of General Virology 14:243–250
    [Google Scholar]
  2. Banker G. A., Cotman C. W. 1972; Measurement of free electrophoretic mobility and retardation of protein-sodium dodecyl sulfate complexes by gel electrophoresis. Journal of Biological Chemistry 247:5856–5861
    [Google Scholar]
  3. Bhatti T., Chambers R. E., Clamp J. R. 1970; The gas chromatographic properties of biologically important N-acetyl glucosamine derivatives, monosaccharides, disaccharides, trisaccharides, tetrasaccharides and pentasaccharides. Biochimica et Biophysica Acta 222:339–347
    [Google Scholar]
  4. Bryce C. F. A., Crichton R. R. 1971; The subunit structure of horse spleen apoferritin. 1. The molecular weight of the subunit. Journal of Biological Chemistry 91:1305–1313
    [Google Scholar]
  5. Burchard R. P., Dworkin M. 1966; A bacteriophage for Myxococcus xanthus: isolation, characterization and relation of infectivity to host morphogenesis. Journal of Bacteriology 91:1305–1313
    [Google Scholar]
  6. Chambers R. E., Clamp J. R. 1971; An assessment of methanolysis and other factors used in the analysis of aldehyde-containing materials. Biochemical Journal 125:1009–1018
    [Google Scholar]
  7. Dworkin M. 1962; Nutritional requirements for vegetative growth of Myxococcus xanthus. Journal of Bacteriology 84:250–257
    [Google Scholar]
  8. Dworkin M., Gibson S. M. 1964; A system for studying microbial morphogenesis: rapid formation of microcysts in Myxococcus xanthus. Science, New York 146:243–244
    [Google Scholar]
  9. Edgar R. S., Wood W. B. 1966; Morphogenesis of bacteriophage T4 in extracts of mutant-infected cells. Proceedings of the National Academy of Sciences of the United States of America 55:498–505
    [Google Scholar]
  10. Gray W. R. 1967; Dansyl chloride procedure. In Methods in Enzymology vol X1 pp. 139–151 Edited by Hirs C. H. W. New York and London: Academic Press;
    [Google Scholar]
  11. Grossman H., Neville D. H. Jun 1971; Glycoproteins of Cell Surfaces. Journal of Biological Chemistry 246:6339–6346
    [Google Scholar]
  12. Hassall H., Soutar A. K. 1974; Amino acid sequence of a peptide containing the active cysteine residue of histidine ammonia-lyase. Biochemical Journal 137:559–566
    [Google Scholar]
  13. Helenius A., Simons K. 1972; The binding of detergents to lipophilic and hydrophilic proteins. Journal of Biological Chemistry 247:3656–3661
    [Google Scholar]
  14. Herriott R. M., Barlow J. L. 1957; The protein coats or ‘ghosts’ of coliphage T2. I. Preparation, assay and some chemical properties. Journal of General Physiology 40:809–825
    [Google Scholar]
  15. Hunt S. 1969; Amino sugars. In Chromatographic and Electrophoretic Techniques Vol I Chromatography, 3rd ed., pp. 784–792 Edited by Smith I. London: Heinemann;
    [Google Scholar]
  16. Katz A. M., Dreyer W. J., Anfinsen C. B. 1959; Peptide separation by two-dimensional chromatography and electrophoresis. The Journal of Biological Chemistry 234:2897–2900
    [Google Scholar]
  17. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227:680–685
    [Google Scholar]
  18. Moody M. F. 1967; Structure of the sheath of bacteriophage T4. I. Structure of the contracted sheath and polysheath. Journal of Molecular Biology 25:167–200
    [Google Scholar]
  19. Nakai N., Lai C. Y., Horecker B. L. 1974; Use of fluorescamine in the chromatographic analysis of peptides from proteins. Analytical Biochemistry 58:563–570
    [Google Scholar]
  20. Parish J. H. 1975; Transfer of drug resistance to Myxococcus from bacteria carrying drug resistance factors. Journal of General Microbiology 87:198–210
    [Google Scholar]
  21. Parish J. H., Kirby J. S. 1966; Reagents which reduce interactions between ribosomal RNA and rapidly labelled RNA from rat liver. Biochimica et Biophysica Acta 129:554–562
    [Google Scholar]
  22. Sarkar N., Sarkar S., Kozloff L. M. 1964; Tail components of T2 bacteriophage. I. Properties of the isolated contractile tail sheath. Biochemistry 3:511–517
    [Google Scholar]
  23. Schroeder W. A. 1967; Separation of peptides by chromatography on columns of Dowex 50 with volatile buffers. In Methods in Enzymology vol X1 pp. 351–361 Edited by Hirs C. H. W. New York and London: Academic Press;
    [Google Scholar]
  24. Sergest J. P., Jackson R. L. 1972; Molecular weight determination of glycoproteins by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. In Methods in Enzymology vol xxvm pp. 54–63 Edited by Ginsberg V. New York and London: Academic Press;
    [Google Scholar]
  25. Simon L. D. 1969; The infection of Escherichia coli by T2 and T4 bacteriophages as seen in the electron microscope. III. Membrane associated intracellular bacteriophages. Virology 38:285–296
    [Google Scholar]
  26. Sonenshein A. L., Roscoe D. H. 1969; The course of phage ϕ e infection in sporulating cells of Bacillus subtilis strain 3610. Virology 39:265–276
    [Google Scholar]
  27. Smyth D. G. 1967; Techniques in enzymic hydrolysis. In Methods in Enzymology vol X1 pp. 214–231 Edited by Hirs C. H. W. New York and London: Academic Press;
    [Google Scholar]
  28. Spiro R. G. 1966; Analysis of sugars found in glycoproteins. In Methods in Enzymology vol VIII pp. 3–26 Edited by Neufeld E. F., Ginsburg V. New York and London: Academic Press;
    [Google Scholar]
  29. Trautman R., Cowan K. M. 1968; Preparative and analytical ultracentrifugation. In Methods in Immunology and Immunochemistry vol II pp. 81–118 Edited by Williams C. A., Chase M. W. New York and London: Academic Press;
    [Google Scholar]
  30. Vinograd J., Hearst J. E. 1962; Equilibrium sedimentation of macromolecules and viruses in a density gradient. Fortschritte der Chemie Organischer Naturstoffe 20:373–422
    [Google Scholar]
  31. Voelz H., Burchard R. P. 1971; Fine structure of bacteriophage-infected Myxococcus xanthus. i. The lytic cycle in vegetative cells. Virology 43:243–250
    [Google Scholar]
  32. Weber K., Osborn M. 1969; The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. Journal of Biological Chemistry 244:4406–4412
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-30-1-99
Loading
/content/journal/jgv/10.1099/0022-1317-30-1-99
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error