1887

Abstract

Polynucleotide phosphorylase activity was demonstrated in free-living and the symbiotic bacteroid forms of and in free-living . Crude extracts of -28 catalysed the polymerization of 3·0 mol ADP (mg protein) h. The polynucleotide phosphorylase activity of symbiotic was about 50 % of that of free-living and remained almost constant throughout the development of the nodules. Partially-purified fractions of free-living -28 catalysed the polymerization of ribonucleoside diphosphates, the phosphorolysis of synthetic homopolymers and natural heteropolymers, and the -phosphate exchange reaction. The enzyme had a pH optimum of 8·0 and had an obligatory requirement for Mg for maximum activity. The phosphorylase was not highly primer-dependent, had low specificity for guanosine-containing substrates, and exhibited cooperative-type kinetics.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-102-2-403
1977-10-01
2024-12-04
Loading full text...

Full text loading...

/deliver/fulltext/micro/102/2/mic-102-2-403.html?itemId=/content/journal/micro/10.1099/00221287-102-2-403&mimeType=html&fmt=ahah

References

  1. Ashwell G. 1957; Colorimetric analysis of sugars. Methods in Enzymology 3:73–105
    [Google Scholar]
  2. Brishammar S., Junto N. 1974; RNA-synthesizing enzymes in healthy and TMV-infected tobacco leaves-partial purification and characterization of tobacco polynucleotide phosphorylase. Archives of Biochemistry and Biophysics 164:224–232
    [Google Scholar]
  3. Chou J. Y., Singer M. F., Mcphie P. 1975; Kinetic studies on the phosphorolysis of polynucleotides by polynucleotide phosphorylase. Journal of Biological Chemistry 250:508–514
    [Google Scholar]
  4. Cowles J. R., Evans H. J. 1968; Some properties of the ribonucleotide reductase from Rhizobium meliloti. . Archives of Biochemistry and Biophysics 127:770–779
    [Google Scholar]
  5. Cowles J. R., Evans H. J., Russell S. A. 1969; B12 Coenzyme-dependent ribonucleotide reductase in rhizobium species and the effects of cobalt deficiency on the activity of the enzyme. Journal of Bacteriology 97:1460–1465
    [Google Scholar]
  6. Davis B. J. 1964; Disc electrophosesis II. Method and application of human serum proteins. Annals of the New York Academy of Sciences 121:404–427
    [Google Scholar]
  7. Dilworth M. J., Williams D. C. 1967; Nucleic acid changes in bacteroids of Rhizobium lupini during nodule development. Journal of General Microbiology 48:31–36
    [Google Scholar]
  8. Fresco J. R., Su D. 1962; Polynucleotides IV. Synthesis of polyriboguanylic acid catalyzed by polynucleotide phosphorylase. Journal of Biological Chemistry 237:3305–3306
    [Google Scholar]
  9. Godefroy-Colburn T., Grunberg-Manago M. 1972; Polynucleotides phosphorylase. In The Enzymes, 3rd edn. 7 pp. 533–574 Edited by Boyer P. D. New York and London: Academic Press;
    [Google Scholar]
  10. Grunberg-Manago M. 1963; Polynucleotide phosphorylase. Progress in Nucleic Acid Research 1:93–133
    [Google Scholar]
  11. Grunberg-Manago M., Ortiz P. J., Ochoa S. 1956; Enzymic synthesis of polynucleotides I. Polynucleotide phosphorylase of Azotobacter vinelandii. . Biochimica et biophysica acta 20:269–285
    [Google Scholar]
  12. Kaplan R., Apirion D. 1975; The fate of ribosomes in Escherichia coli cells starved for a carbon source. Journal of Biological Chemistry 250:1854–1863
    [Google Scholar]
  13. Kimhi Y., Littauer U. Z. 1968; Purification and properties of polynucleotide phosphorylase from Escherichia coli. . Journal of Biological Chemistry 243:231–240
    [Google Scholar]
  14. Kinscherf T. B., Apirion D. 1975; Polynucleotide phosphorylase can participate in decay of mRNA in Escherichia coli in the absence of ribonuclease II. Molecular and General Genetics 139:357–362
    [Google Scholar]
  15. Kirby K. 1965; Isolation and characterization of ribosomal ribonucleic acid. Biochemical Journal 96:266–269
    [Google Scholar]
  16. Kunitz M. 1946; A spectrophotometric method for the measurement of ribonuclease activity. Journal of Biological Chemistry 164:563–568
    [Google Scholar]
  17. Kunitz M. 1950; Crystalline desoxyribonucleasel. Isolation and general properties: spectrophotometric method for the measurement of desoxy-ribonuclease activity. Journal of General Physiology 33:349–362
    [Google Scholar]
  18. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
  19. Ochoa S., Krakow J. S., Basilio C. 1965; Polynucleotide phosphorylase from Azobacter vinelandii. . Methods in Enzymology 6:3–11
    [Google Scholar]
  20. Ornstein L. 1964; Disc electrophoresis I. Background and theory. Annals of the New York Academy of Sciences 121:321–349
    [Google Scholar]
  21. Paau A., Cowles J. R. 1975; Comparison of DNA polymerase of Rhizobium meliloti and alfalfa bacteroids. Plant Physiology 56:526–528
    [Google Scholar]
  22. Rokugawa K., Katoh Y., Kuninaka A., Yoshino H. 1975; Polynucleotide phosphorylase from Achromobacter sp. KR 170-4. Agricultural and Biological Chemistry 39:1455–1460
    [Google Scholar]
  23. See Y. P., Fitt P. S. 1972; Partial purification and properties of rat liver mitochondrial polynucleotide phosphorylase. Biochemical Journal 130:343–353
    [Google Scholar]
  24. Segel I. H. 1975 Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady State Enzyme Systems pp. 380–381 New York: John Wiley;
    [Google Scholar]
  25. Sugino Y., Miyoshi Y. 1967; The specific precipitation of orthophosphate and some biochemical applications. Journal of Biological Chemistry 239:2360–2364
    [Google Scholar]
  26. Thang M. N., Thang D. C., Leautey J. 1967; Physicochimie biologique - séparation et identification de polynucleotide phosphorylase per electrophorése sur gel polyacrylamide. Comptes rendus hebdomadaire des seances de TAcademie des sciences 265:1823–1826
    [Google Scholar]
  27. 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]
/content/journal/micro/10.1099/00221287-102-2-403
Loading
/content/journal/micro/10.1099/00221287-102-2-403
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