The Cell Membrane of Mycoplasmas

  • Shmuel Razin


Most mycoplasmologists support the proposal of Gibbons and Murray (1978) endowing the mycoplasmas with the lofty status of one of the four major divisions in the kindgom Procaryotae, the division named Mollicutes (mollis soft + cutes skin) to denote the lack of cell walls in these organisms. The recent report that penicillin-binding proteins and enzymes of peptidoglycan synthesis are absent from mycoplasmas as against their presence in the plasma membrane of the wall-less bacterial L-forms (Martin et al., 1980) supports the idea of a separate division for mycoplasmas. A different view has recently been expressed by Fox et al. (1980) who, on the basis of nucleotide sequences in 16 S rRNA, argue that mycoplasmas are genealogically wall-less descendents of clostridia, and consequently should not be given a separate high taxonomic status. Notwithstanding this somewhat philosophical controversy, the fact is that mycoplasmas differ from other prokaryotes in several unique properties, most useful in membrane studies. Thus, the mycoplasmas are unique in being the only self-replicating organisms with a single membranous structure—the plasma membrane. This is, perhaps, their greatest advantage in membrane studies, for it facilitates the isolation of pure plasma membranes uncontaminated by other membrane types. Moreover, the mycoplasmas’ lack of cell walls enables the application of gentle and simple techniques, such as osmotic lysis for membrane isolation (Razin, 1978, 1981).


Membrane Fluidity Ureaplasma Urealyticum Peptidoglycan Synthesis Lipid Phase Transition Membrane Study 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Amar, A., Rottem, S., and Razin, S. (1978). Biochem. Biophys. Res. Commun. 84, 306–312.CrossRefGoogle Scholar
  2. Banai, M., Razin, S., Bredt, W., and Kahane, I. (1980). Infect. Immun. 30, 628–634.Google Scholar
  3. Bevers, E. M., Singal, S. A., Kamp, J. A. F., and van Deenen, L. L. M. (1977). Biochemistry 16, 1290–1295.CrossRefGoogle Scholar
  4. Cirillo, V. P. (1979). In The Mycoplasmas (M. F. Barile and S. Razin, eds.), Vol. I, pp. 323–349, Academic Press, New York.Google Scholar
  5. Clejan, S., Bittman, R., and Rottem, S. (1981). Biochemistry, 20, 2200–2206.CrossRefGoogle Scholar
  6. Dahl, J. S., Dahl, C. E., and Bloch, K. (1980). Biochemistry 19, 1467–1471.CrossRefGoogle Scholar
  7. Dahl, J. S., Dahl, C. E., and Bloch, K. (1981). J. Biol. Chem. 256. 87–91.Google Scholar
  8. Daniels, M. J., Longland, J. M., and Gilbert, J. (1980). J. Gen. Microbiol. 118, 429–436.Google Scholar
  9. Efrati, H., Rottem, S., and Razin, S. (1981). Biochim. Biophys. Acta, 641, 386–394.CrossRefGoogle Scholar
  10. Feldner, J., Bredt, W., and Razin, S. (1981). Infect. Immun., 31, 107–113.Google Scholar
  11. Fox, G. E., Stackebrandt, E., Hespell, R. B., Gibson, J., Maniloff, J., Dyer, T. A., Wolfe, R. S., Balch, W. E., Tanner, R. S., Magrum, L. J., Zablen, L. B., Blakemore, R., Gupta, R., Bonen, L., Lewis, B. J., Stahl, D. A., Luehersen, K. R., Chen, K. N., and Woese, C. R. (1980). Science 209, 457–463.CrossRefGoogle Scholar
  12. Gibbons, N. E., and Murray, R. G. E. (1978). Int. J. Syst. Bacteriol. 28, 1–6.CrossRefGoogle Scholar
  13. Gross, Z., and Rottem, S. (1979). Biochim. Biophys. Acta 555, 547–552.CrossRefGoogle Scholar
  14. Hu, P. C., Collier, A. M., and Baseman, J. B. (1977). J. Exp. Med. 145, 1328–1343.CrossRefGoogle Scholar
  15. Johansson, K.-E., Pertoft, H., and Hjerten, S. (1979). Int. J. Biol. Macromol. 1, 111–118.CrossRefGoogle Scholar
  16. Kahane, I., and Brunner, H. (1977). Infect. Immun. 18, 273–277.Google Scholar
  17. Leblanc, G., and Le Grimellec, C. (1979). Biochim. Biophys. Acta 554, 168–179.CrossRefGoogle Scholar
  18. Le Grimellec, C., Lajeunesse, D., and Rigaud, J.L. (1982). Rev. Infect. Dis., in press.Google Scholar
  19. McElhaney, R. N. (1974). J. Mol. Biol. 84, 145–157.CrossRefGoogle Scholar
  20. Martin, H. H., Schilf, W., and Schiefer, H.-G. (1980). Arch. Microbiol. 127, 297–299.CrossRefGoogle Scholar
  21. Melchior, D. L., and Rattern, S. (1981). Eur. J. Biochem. 117, 147–153.CrossRefGoogle Scholar
  22. Meng, K. E., and Pfister, R. M. (1980). J. Bacteriol. 144, 390–399.Google Scholar
  23. Neimark, H. C. (1977). Proc. Natl. Acad. Sci. USA 74, 4041–4045.CrossRefGoogle Scholar
  24. Odriozola, J. M., Waitzkin, E., Smith, T. L., and Bloch, K. (1978). Proc. Natl. Acad. Sci. USA 75, 4107–4109.CrossRefGoogle Scholar
  25. Razin, S. (1978). Microbiol. Rev. 42, 414–470.Google Scholar
  26. Razin, S. (1981). In Organization of Prokaryotic Cell Membranes (B. K. Ghosh, ed.), Vol. I, pp. 180–273, CRC Press, Boca Raton, Fla.Google Scholar
  27. Razin, S., Kutner, S., Efrati, H., and Rottem, S. (1980). Biochim. Biophys. Acta 598, 628–640.CrossRefGoogle Scholar
  28. Rodwell, A. W. (1968). Science 160, 1350–1351.CrossRefGoogle Scholar
  29. Romano, N., Tolone, G., Ajello, F., and Licata, R. L. (1980). J. Bacteriol. 144, 830–832.Google Scholar
  30. Rottem, S., and Markowitz, O. (1979). FEBS Lett. 107, 379–382.CrossRefGoogle Scholar
  31. Rottem, S., Linker, C., and Wilson, T. H. (1981). J. Bacteriol., 145, 1299–1304.Google Scholar
  32. Schummer, U., Schiefer, H.-G., and Gerhardt, U. (1980). Biochim. Biophys. Acta 600, 998–1006.CrossRefGoogle Scholar
  33. Silvius, J. R., and McElhaney, R. N. (1980). Proc. Natl. Acad. Sci. USA 77, 1255–1259.CrossRefGoogle Scholar
  34. Silvius, J. R., Mak, N., and McElhaney, R. N. (1980). Biochim. Biophys. Acta 597, 199–215.CrossRefGoogle Scholar
  35. Slutzky, G. M., Razin, S., Kahane, I., and Eisenberg, S. (1977). Biochemistry 16, 5158–5163.CrossRefGoogle Scholar
  36. Smith, M. W. (1980). Ph.D. thesis, Brown University, Providence.Google Scholar
  37. Stanbridge, E. J., and Weiss, R. L. (1978). Nature (London) 276, 583–587.CrossRefGoogle Scholar
  38. Tarshis, M. A., and Kapitanov, A. B. (1978). FEBS Lett. 89, 73–77.CrossRefGoogle Scholar
  39. Townsend, R., Archer, D. B., and Plaskitt, K. A. (1980). J. Bacteriol. 142, 694–700.Google Scholar
  40. Wieslander, A., Christiansson, A., Rilfors, L., and Lindblom, G. (1980). Biochemistry 19, 3650–3655.CrossRefGoogle Scholar
  41. Williamson, D. L., Blaustein, D. I., Levine, R. J. C., and Elfvin, M. J. (1979). Curr. Microbiol. 2, 143–145.CrossRefGoogle Scholar
  42. Wise, K. S., Cassell, G. H., and Acton, R. T. (1978). Proc. Natl. Acad. Sci. USA 75, 4479–4483.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • Shmuel Razin
    • 1
  1. 1.Department of Membrane and Ultrastructure ResearchThe Hebrew University-Hadassah Medical SchoolJerusalemIsrael

Personalised recommendations