Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1977 Sep;74(9):4041–4045. doi: 10.1073/pnas.74.9.4041

Extraction of an actin-like protein from the prokaryote Mycoplasma pneumoniae.

H C Neimark
PMCID: PMC431835  PMID: 333456

Abstract

An actin-like protein has been identified in cell extracts from the prokaryote Mycoplasma pneumoniae. This protein bears a striking resemblance to actin from vertebrates: (i) the solubility of the protein during isolation is analogous to that of actin bound to myosin (soluble in high ionic strength salt solution and insoluble at low ionic strength), (ii) sodium dodecyl sulfate treatment of the partially purified M. pneumoniae extract produces a protein with an electrophoretic mobility very close to that of vertebrate actin in sodium dodecyl sulfate/polyacrylamide gels, (iii) treatment of preparations with ATP-Mg2+ allows separation of long curvilinear filaments, 5-6 nm wide, that closely resemble eukaryotic filamentous actin, and (iv) the prokaryotic filamentous actin binds vertebrate heavy meromyosin fragments to form hybrid compleexes with the characteristic shape of periodic repeating arrowheads, and no heavy meromyosin is bound in the presence of ATP.

Full text

PDF
4041

Images in this article

4042Image
on p.4042
4043Image
on p.4043
4043Image
on p.4043
4043Image
on p.4043

Selected References

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

  1. Abramowitz J., Stracher A., Detwiler T. The differential effect of Ca-ATP and Mg-ATP on platelet actomyosin. Biochem Biophys Res Commun. 1972 Nov 15;49(4):958–963. doi: 10.1016/0006-291x(72)90305-1. [DOI] [PubMed] [Google Scholar]
  2. Adelstein R. S., Pollard T. D., Kuehl W. M. Isolation and characterization of myosin and two myosin fragments from human blood platelets. Proc Natl Acad Sci U S A. 1971 Nov;68(11):2703–2707. doi: 10.1073/pnas.68.11.2703. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Allison A. C., Davies P., De Petris S. Role of contractile microfilaments in macrophage movement and endocytosis. Nat New Biol. 1971 Aug 4;232(31):153–155. doi: 10.1038/newbio232153a0. [DOI] [PubMed] [Google Scholar]
  4. Bak A. L., Black F. T., Christiansen C., Freundt E. A. Genome size of mycoplasmal DNA. Nature. 1969 Dec 20;224(5225):1209–1210. doi: 10.1038/2241209a0. [DOI] [PubMed] [Google Scholar]
  5. Bettex-Galland M., Lüscher E. F. Thrombosthenin, the contractile protein from blood platelets and its relation to other contractile proteins. Adv Protein Chem. 1965;20:1–35. doi: 10.1016/s0065-3233(08)60387-3. [DOI] [PubMed] [Google Scholar]
  6. Biberfeld G., Biberfeld P. Ultrastructural features of Mycoplasma pneumoniae. J Bacteriol. 1970 Jun;102(3):855–861. doi: 10.1128/jb.102.3.855-861.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Chanock R. M. Mycoplasma infections of man. N Engl J Med. 1965 Nov 25;273(22):1199–contd. doi: 10.1056/NEJM196511252732206. [DOI] [PubMed] [Google Scholar]
  8. Collier A. M., Clyde W. A., Jr Appearance of Mycoplasma pneumoniae in lungs of experimentally infected hamsters and sputum from patients with natural disease. Am Rev Respir Dis. 1974 Dec;110(6):765–773. doi: 10.1164/arrd.1974.110.6P1.765. [DOI] [PubMed] [Google Scholar]
  9. Doetsch R. N., Hageage G. J. Motility in procaryotic organisms: problems, points of view, and perspectives. Biol Rev Camb Philos Soc. 1968 Aug;43(3):317–362. doi: 10.1111/j.1469-185x.1968.tb00963.x. [DOI] [PubMed] [Google Scholar]
  10. Dreizen P., Hartshorne D. J., Stracher A. The subunit structure of myosin. I. Polydispersity in 5 M guanidine. J Biol Chem. 1966 Jan 25;241(2):443–448. [PubMed] [Google Scholar]
  11. Fairbanks G., Jr, Levinthal C., Reeder R. H. Analysis of C14-labeled proteins by disc electrophoresis. Biochem Biophys Res Commun. 1965 Aug 16;20(4):393–399. doi: 10.1016/0006-291x(65)90589-9. [DOI] [PubMed] [Google Scholar]
  12. Gabbiani G., Ryan G. B., Lamelin J. P., Vassalli P., Majno G., Bouvier C. A., Cruchaud A., Lüscher E. F. Human smooth muscle autoantibody. Its identification as antiactin antibody and a study of its binding to "nonmuscular" cells. Am J Pathol. 1973 Sep;72(3):473–488. [PMC free article] [PubMed] [Google Scholar]
  13. Harmon J. M., Taber H. W. Altered accumulation of a membrane protein unique to a membrane-deoxyribonucleic acid complex in a dna initiation mutant of Bacillus subtilis. J Bacteriol. 1977 Jun;130(3):1224–1233. doi: 10.1128/jb.130.3.1224-1233.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Henrichsen J. Gliding and twitching motility of bacteria unaffected by cytochalasin B. Acta Pathol Microbiol Scand B Microbiol Immunol. 1972;80(4):623–624. doi: 10.1111/j.1699-0463.1972.tb00187.x. [DOI] [PubMed] [Google Scholar]
  15. Jahn T. L., Bovee E. C. Movement and locomotion of microorganisms. Annu Rev Microbiol. 1965;19:21–58. doi: 10.1146/annurev.mi.19.100165.000321. [DOI] [PubMed] [Google Scholar]
  16. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  17. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  18. Lazarides E., Lindberg U. Actin is the naturally occurring inhibitor of deoxyribonuclease I. Proc Natl Acad Sci U S A. 1974 Dec;71(12):4742–4746. doi: 10.1073/pnas.71.12.4742. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Lowey S., Slayter H. S., Weeds A. G., Baker H. Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation. J Mol Biol. 1969 May 28;42(1):1–29. doi: 10.1016/0022-2836(69)90483-5. [DOI] [PubMed] [Google Scholar]
  20. Maniloff J., Morowitz H. J., Barrnett R. J. Ultrastructure and Ribosomes of Mycoplasma gallisepticum. J Bacteriol. 1965 Jul;90(1):193–204. doi: 10.1128/jb.90.1.193-204.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Minkoff L., Damadian R. Actin-like properties from Escherichia coli: concept of cytotonus as the missing link between cell metabolism and the biological ion-exchange resin. J Bacteriol. 1976 Jan;125(1):353–365. doi: 10.1128/jb.125.1.353-365.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Morowitz H. J., Bode H. R., Kirk R. G. The nucleic acids of mycoplasma. Ann N Y Acad Sci. 1967 Jul 28;143(1):110–114. doi: 10.1111/j.1749-6632.1967.tb27650.x. [DOI] [PubMed] [Google Scholar]
  23. Offer G., Moos C., Starr R. A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization. J Mol Biol. 1973 Mar 15;74(4):653–676. doi: 10.1016/0022-2836(73)90055-7. [DOI] [PubMed] [Google Scholar]
  24. Perry M. M., John H. A., Thomas N. S. Actin-like filaments in the cleavage furrow of newt egg. Exp Cell Res. 1971 Mar;65(1):249–253. doi: 10.1016/s0014-4827(71)80075-7. [DOI] [PubMed] [Google Scholar]
  25. Rosenbusch J. P., Jacobson G. R., Jaton J. C. Does a bacterial elongation factor share a common evolutionary ancestor with actin? J Supramol Struct. 1976;5(3):391–396. doi: 10.1002/jss.400050311. [DOI] [PubMed] [Google Scholar]
  26. Spudich J. A., Watt S. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem. 1971 Aug 10;246(15):4866–4871. [PubMed] [Google Scholar]
  27. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  28. Weltman J. K., Dowben R. M. Relatedness among contractile and membrane proteins: evidence for evolution from common ancestral genes. Proc Natl Acad Sci U S A. 1973 Nov;70(11):3230–3234. doi: 10.1073/pnas.70.11.3230. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES