1887

Abstract

Purified adenosine triphosphatase (F-ATPase) (EC 3.6.1.3) from membranes required divalent metal ions for its reattachment to membranes depleted of the enzyme. This requirement showed specificity: Mg ions were able to reconstitute a physiologically significant F-ATPase-membrane complex, whereas Zn ions produced one differing from the native and the Mg-reconstituted ATPase-membrane complexes. membranes contained a limited number of specific binding sites, which did not seem to be modified after ATPase release and membrane manipulation. The binding properties of F-ATPase preparations correlated well with their content of δ-subunit. The results suggested that F-ATPase molecules able to rebind to membranes must contain at least two copies of the δ-subunit. The isolated subunits (particularly α- and β-subunits) showed a certain capacity for rebinding to the membranes, but an enzyme form consisting only of α- and β-subunits was unable to reattach to membranes. These results prove unambiguously that δ-, but not α-or any other polypeptide, was involved in the attachment of F-ATPase to membranes, unlike other bacterial F-ATPases. These results were consistent with a subunit stoichiometry and arrangement: α β γ δ-Mg- membrane.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-129-11-3465
1983-11-01
2021-07-29
Loading full text...

Full text loading...

/deliver/fulltext/micro/129/11/mic-129-11-3465.html?itemId=/content/journal/micro/10.1099/00221287-129-11-3465&mimeType=html&fmt=ahah

References

  1. Abrams A., Baron C. 1968; Reversible attachment of adenosine triphosphatase to streptococcal membranes and the effect of magnesium ions. Biochemistry 7:501–507
    [Google Scholar]
  2. Abrams A., Smith J.B. 1974; Bacterial membranes ATPase. In The Enzymes X: pp. 395–429 Edited by Boyer P.D. New York & London: Academic Press;
    [Google Scholar]
  3. Abrams A., Jensen C., Morris D.H. 1976a; Role of Mg2+ ions in the subunit structure and membrane binding properties of bacterial energy transducing ATPase. Biochemical and Biophysical Research Communications 69:804–811
    [Google Scholar]
  4. Abrams A., Morris D., Jensen C. 1976b; Chymotryptic conversion of bacterial membrane ATPase to an active form with modified a chains and defective membrane binding properties. Biochemistry 15:5560–5566
    [Google Scholar]
  5. Andreu J.M., Muñoz E. 1975; Micrococcus lysodeikticus ATPase. Purification by preparative gel electrophoresis and subunit structure studied by urea and sodium dodecylsulfate gel electrophoresis. Biochimica et biophysica acta 387:228–233
    [Google Scholar]
  6. Andreu J.M., Muñoz E. 1979; Molecular properties of random coil and refolded forms of α and β subunits of an energy transducing ATPase from bacterial membranes. Biochemistry 18:1836–1844
    [Google Scholar]
  7. Andreu J.M., Albendea J.A., Muñoz E. 1973; Membrane adenosine triphosphatase ofMicrococcus lysodeikticus. Molecular properties of the purified enzyme unstimulated by trypsin. European Journal of Biochemistry 37:505–515
    [Google Scholar]
  8. Andreu J.M., Carreira J., Muñoz E. 1976; Isolation and partial characterization of the two major subunits of BFj factor (ATPase) fromMicrococcus lysodeikticus and evidence of their glycoprotein nature. FEBS Letters 65:198–203
    [Google Scholar]
  9. Carreira J., Andreu J.M., Muñoz E. 1977; Differential sensitivity to trypsin digestion of purified forms ofMicrococcus lysodeikticus ATPase (BF1). A study of their structural and conformational differences and mechanism of conversion. Biochimica et biophysica acta 492:387–398
    [Google Scholar]
  10. Cross R.L. 1981; The mechanism and regulation of ATP synthesis by F1-ATPases. Annual Review of Biochemistry 50:681–714
    [Google Scholar]
  11. Dietzel W., Koppershlager C., Hoffman E. 1972; An improved procedure for protein staining in polyacrylamide gels with a new type of Coomassie brillant blue. Analytical Biochemistry 48:617–620
    [Google Scholar]
  12. Downie J.A., Gibson F., Cox G.B. 1979; Membrane adenosine triphosphatases of prokaryotic cells. Annual Review of Biochemistry 48:103–131
    [Google Scholar]
  13. Eytan G.D., Matheson M.T. 1976; Incorporation of mitochondrial membrane proteins into liposomes containing acid phospholipids. Journal of Biological Chemistry 251:6831–6837
    [Google Scholar]
  14. Fairbanks G., Steck T.L., Wallach D.F.H. 1971; Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606–2617
    [Google Scholar]
  15. Greenwood F.C., Hunter W.M., Glover S.J. 1963; The preparation of131I-labelled human growth hormone of high specific radioactivity. Biochemical Journal 89:114–123
    [Google Scholar]
  16. Larraga V., Mollinedo F., Rubio N., Muñoz E. 1981; Influence of the α-, β- and γ-subunits of the energy-transducing adenosine triphosphatase fromMicrococcus lysodeikticus in the immunochemical properties of the protein and in their reconstitution studied by a radioimmunoassay method. Biochemical Journal 193:729–735
    [Google Scholar]
  17. Leimgruber R.M., Jensen C., Abrams A. 1978; Accessibility of the α-chains in membrane-bound and solubilized bacterial ATPase to chymotryptic cleavage. Biochemical and Biophysical Research Communications 81:439–447
    [Google Scholar]
  18. Matthews B.W. 1982; Lipid-protein interactions in a bacteriochlorophyll-containing protein. In Lipid- Protein Interactions 11–23 Edited by Jost P.C., Griffith D.H. New York: John Wiley;
    [Google Scholar]
  19. Mimbrera A., Rivas L., Mollinedo F., Muñoz E., Larraga V. 1983; Topography of the subunits ofMicrococcus lysodeikticus F,-ATPase. Molecular and Cellular Biochemistry 56:73–80
    [Google Scholar]
  20. Mollinedo F., Larraga V., Coll F.J., Muñoz E. 1980; Role of the subunits of the energy- transducing adenosine triphosphatase fromMicrococcus lysodeikticus membranes, studied by proteolytic digestion and immunological approaches. Biochemical Journal 186:713–723
    [Google Scholar]
  21. Mollinedo F., Lopez-Moratalla N., Pivel J.P., Larraga V., Santiago E., Muñoz E. 1981; Identification of a bacterial energy-transducing ATPase as a metallo (Zn2 + ) protein. Effect of chelating agents and divalent metal ions on ATPase activity. European Journal of Biochemistry 119:183–188
    [Google Scholar]
  22. Muñoz E. 1982; Polymorphism and conformational dynamics of F1-ATPases from bacterial membranes. A model for the regulation of these enzymes on the basis of molecular plasticity. Biochimica et biophysica acta 650:233–265
    [Google Scholar]
  23. Muñoz E., Freer J. H., Ellar D. J., Salton M. R. J. 1968a; Membrane-associated ATPase activity fromMicrococcus lysodeikticus. . Biochimica et biophysica acta 150:531–533
    [Google Scholar]
  24. Muñoz E., Nachbar M. S., Schor M. T., Salton M. R. J. 1968b; Adenosine triphosphatase ofMicrococcus lysodeikticus: selective release and relationship to membrane structure. Biochemical and Biophysical Research Communications 32:539–546
    [Google Scholar]
  25. Muñoz E., Salton M.R.J., Ng M.H., Schor M.T. 1969; Membrane adenosine triphosphatase ofMicrococcus lysodeikticus. Purification, properties of the ‘soluble’ enzyme and properties of the membrane-bound enzyme. European Journal of Biochemistry 7:490–501
    [Google Scholar]
  26. Muñoz E., Palacios P., Marquet A., Andreu J.M. 1980; Substructure of F1-ATPase (BF1 factor) fromMicrococcus lysodeikticus. . Molecular Cellular Biochemistry 33:3–12
    [Google Scholar]
  27. Nelson N. 1976; Structure and function of chloro- plast ATPase. Biochimica et biophysica acta 456:314–338
    [Google Scholar]
  28. Penefsky H.S. 1979; Mitochondrial ATPase. Advances in Enzymology 49:223–280
    [Google Scholar]
  29. Senior A.E. 1973; The structure of mitochondrial ATPase. Biochimica et biophysica acta 301:249–277
    [Google Scholar]
  30. Shavit N. 1980; Energy transduction in chloro- plasts: structure and function of the ATPase complex. Annual Review of Biochemistry 49:111–138
    [Google Scholar]
  31. Sone N., Yoshida M., Hirata H., Kagawa Y. 1977; Reconstitution of vesicles capable of energy transformation from phospholipids and adenosine triphosphatase of a thermophilic bacterium. Journal of Biochemistry 81:519–528
    [Google Scholar]
  32. Sternweis P.C. 1978; The subunit of Escherichia coli coupling factor 1 is required for its binding to the cytoplasmic membrane. Journal of Biological Chemistry 253:3123–3128
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-129-11-3465
Loading
/content/journal/micro/10.1099/00221287-129-11-3465
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