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. 1990 May;172(5):2808–2811. doi: 10.1128/jb.172.5.2808-2811.1990

A 57-kilodalton protein associated with Spiroplasma melliferum fibrils undergoes reversible phosphorylation.

M W Platt 1, J Reizer 1, S Rottem 1
PMCID: PMC208935  PMID: 2332410

Abstract

Phosphorylation of a major 57-kilodalton protein substrate was observed in cell lysates of Spiroplasma melliferum BC3 incubated with [gamma-32P]ATP. Only serine phosphates have been isolated from the acid hydrolysate of the phosphorylated protein. The 57-kilodalton protein substrate was found, to a large extent, in the cytosolic fraction and, to a lesser extent, associated with cell membranes and was detected in the Triton X-100-insoluble fraction that contained fibrils.

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Selected References

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  1. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  2. Cohen P. The role of protein phosphorylation in the hormonal control of enzyme activity. Eur J Biochem. 1985 Sep 16;151(3):439–448. doi: 10.1111/j.1432-1033.1985.tb09121.x. [DOI] [PubMed] [Google Scholar]
  3. Deutscher J., Saier M. H., Jr ATP-dependent protein kinase-catalyzed phosphorylation of a seryl residue in HPr, a phosphate carrier protein of the phosphotransferase system in Streptococcus pyogenes. Proc Natl Acad Sci U S A. 1983 Nov;80(22):6790–6794. doi: 10.1073/pnas.80.22.6790. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fischer M., Shirvan M. H., Platt M. W., Kirchhoff H., Rottem S. Characterization of membrane components of the flask-shaped mycoplasma Mycoplasma mobile. J Gen Microbiol. 1988 Aug;134(8):2385–2392. doi: 10.1099/00221287-134-8-2385. [DOI] [PubMed] [Google Scholar]
  5. Göbel U., Speth V., Bredt W. Filamentous structures in adherent Mycoplasma pneumoniae cells treated with nonionic detergents. J Cell Biol. 1981 Nov;91(2 Pt 1):537–543. doi: 10.1083/jcb.91.2.537. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hunter T. A thousand and one protein kinases. Cell. 1987 Sep 11;50(6):823–829. doi: 10.1016/0092-8674(87)90509-5. [DOI] [PubMed] [Google Scholar]
  7. Inagaki M., Gonda Y., Matsuyama M., Nishizawa K., Nishi Y., Sato C. Intermediate filament reconstitution in vitro. The role of phosphorylation on the assembly-disassembly of desmin. J Biol Chem. 1988 Apr 25;263(12):5970–5978. [PubMed] [Google Scholar]
  8. Kirchhoff H., Rosengarten R., Lotz W., Fischer M., Lopatta D. Flask-shaped mycoplasmas: properties and pathogenicity for man and animals. Isr J Med Sci. 1984 Sep;20(9):848–853. [PubMed] [Google Scholar]
  9. Krebs E. G., Beavo J. A. Phosphorylation-dephosphorylation of enzymes. Annu Rev Biochem. 1979;48:923–959. doi: 10.1146/annurev.bi.48.070179.004423. [DOI] [PubMed] [Google Scholar]
  10. Neimark H. Mycoplasma and bacterial proteins resembling contractile proteins: a review. Yale J Biol Med. 1983 Sep-Dec;56(5-6):419–423. [PMC free article] [PubMed] [Google Scholar]
  11. Parkinson J. S. Protein phosphorylation in bacterial chemotaxis. Cell. 1988 Apr 8;53(1):1–2. doi: 10.1016/0092-8674(88)90478-3. [DOI] [PubMed] [Google Scholar]
  12. Platt M. W., Rottem S., Milner Y., Barile M. F., Peterkofsky A., Reizer J. Protein phosphorylation in Mycoplasma gallisepticum. Eur J Biochem. 1988 Sep 1;176(1):61–67. doi: 10.1111/j.1432-1033.1988.tb14251.x. [DOI] [PubMed] [Google Scholar]
  13. Platt M. W., Rottem S. Phosvitin kinase activity in Acholeplasma axanthum. FEBS Lett. 1988 Dec 19;242(1):97–100. doi: 10.1016/0014-5793(88)80993-1. [DOI] [PubMed] [Google Scholar]
  14. Razin S. The mycoplasmas. Microbiol Rev. 1978 Jun;42(2):414–470. doi: 10.1128/mr.42.2.414-470.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Reizer J., Saier M. H., Jr, Deutscher J., Grenier F., Thompson J., Hengstenberg W. The phosphoenolpyruvate:sugar phosphotransferase system in gram-positive bacteria: properties, mechanism, and regulation. Crit Rev Microbiol. 1988;15(4):297–338. doi: 10.3109/10408418809104461. [DOI] [PubMed] [Google Scholar]
  16. Saha A. K., Dowling J. N., Mukhopadhyay N. K., Glew R. H. Demonstration of two protein kinases in extracts of Legionella micdadei. J Gen Microbiol. 1988 May;134(5):1275–1281. doi: 10.1099/00221287-134-5-1275. [DOI] [PubMed] [Google Scholar]
  17. Szczesna D., Sobieszek A., Kakol I. Binding of phosphorylated and dephosphorylated heavy meromyosin to F-actin. FEBS Lett. 1987 Jan 5;210(2):177–180. doi: 10.1016/0014-5793(87)81332-7. [DOI] [PubMed] [Google Scholar]
  18. Townsend R., Archer D. B., Plaskitt K. A. Purification and preliminary characterization of Spiroplasma fibrils. J Bacteriol. 1980 May;142(2):694–700. doi: 10.1128/jb.142.2.694-700.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Wang J. Y., Koshland D. E., Jr Evidence for protein kinase activities in the prokaryote Salmonella typhimurium. J Biol Chem. 1978 Nov 10;253(21):7605–7608. [PubMed] [Google Scholar]
  20. Williamson D. L. Unusual fibrils from the spirochete-like sex ratio organism. J Bacteriol. 1974 Feb;117(2):904–906. doi: 10.1128/jb.117.2.904-906.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]

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