Advertisement

Journal of Muscle Research & Cell Motility

, Volume 7, Issue 2, pp 97–109 | Cite as

The reconstruction of myosin filaments in rabbit psoas muscle from solubilized myosin

  • Maria C. Maw
  • Arthur J. Rowe
Papers

Summary

Using rabbit psoas muscle strips, A-bands with their myosin-containing thick filaments have been substantially reconstructedin situ (as judged by electron and light microscopy and by low-angle X-ray diffraction analysis) after prior solubilization of the myosin filaments in high ionic strength potassium phosphate solution. The maintenance of a very high local concentration of soluble myosin, by means of a closely apposed artificial semi-permeable membrane is necessary for reconstruction of full-length filaments. This reconstruction effect can be totally abolished by pre-glycerolation of the muscle, or (reversibly) by pre-depletion of Ca2+. Reconstruction at longer sarcomere lengths (>2.6μm) is anomalous, part-length ‘stub filaments’ being formed, with their stub tails projecting out from the I-Z-I lattice. A model is proposed to explain this reconstruction effect.

Keywords

Ionic Strength Diffraction Analysis Potassium Phosphate Local Concentration High Ionic Strength 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Burke, M. &Harrington, W. F. (1972) Geometry of the myosin dimer in high-salt media. II. Hydrodynamic studies on macromodels of myosin and its rod fragments.Biochemistry 11, 1456–62.Google Scholar
  2. Craig, R. &Offer, G. (1976) The location of C-protein in rabbit skeletal muscle.Proc. R. Soc. Ser. B. 192, 451–61.Google Scholar
  3. Davis, J. S., Buck, J. &Greene, E. P. (1982) The myosin dimer: an intermediate in the self-assembly of the thick filament of vertebrate skeletal muscle.FEBS Lett. 140, 293–7.Google Scholar
  4. Dos Remedios, C. G. &Gilmour, D. (1978) Is there a third type of filament in striated muscles?J. Biochem. 84, 235–8.Google Scholar
  5. Durham, A. C., Finch, J. T. &Klug, A. (1971) States of aggregation of tobacco mosaic virus protein.Nature, New Biol. 229, 37–42.Google Scholar
  6. Durham, A. C. &Klug, A. (1971) Polymerisation of tobacco mosaic virus protein and its control.Nature, New Biol. 229, 42–7.Google Scholar
  7. Emes, C. H. (1978)Myofilament and molecule: a study on myosin. Ph.D. Thesis, University of Leicester, Leicester, U.K.Google Scholar
  8. Emes, C. H. &Rowe, A. J. (1978) Frictional properties and molecular weight of native and synthetic myosin filaments from vertebrate skeletal muscle.Biochim. biophys. Acta 537, 125–44.Google Scholar
  9. Hattori, A. &Takahashi, K. (1979) Studies on the post-mortem fragmentation of myofibrils.J. Biochem. 85, 47–56.Google Scholar
  10. Hodgkin, A. L. &Horowicz, P. (1957) The influence of potassium and chloride ions on the membrane potential of single muscle fibres.J. Physiol., Lond. 148, 127–60.Google Scholar
  11. Huxley, H. E. (1963) Electron microscopic studies on the structure of natural and synthetic protein filaments from striated muscle.J. molec. Biol. 7, 281–308.Google Scholar
  12. Huxley, A. F. &Simmons, R. M. (1972) Proposed mechanism of force generation in striated muscle.Nature, Lond. 233, 533–8.Google Scholar
  13. Kaminer, B. &Bell, A. L. (1966) Myosin filamentogenesis: effects of pH and ionic concentration.J. molec. Biol. 20, 391–401.Google Scholar
  14. Katsura, I. &Noda, H. (1971) Studies on the formation and physical chemical properties of synthetic myosin filaments.J. Biochem. 69, 219–29.Google Scholar
  15. Katsura, I. &Noda, H. (1973) Further studies on the formation of reconstituted myosin Filaments,J. Biochem. 73, 245–56.Google Scholar
  16. Koretz, J. F. (1979a) Structural studies of synthetic filaments prepared from column-purified myosin.Biophys. J. 27, 423–32.Google Scholar
  17. Koretz, J. F. (1979b) Effects of C-protein on synthetic myosin filament structure.Biophys. J. 27, 433–46.Google Scholar
  18. Lazarides, E. &Granger, B. L. (1978) Fluorescent localisation of membrane sites in glycerinated chicken skeletal muscle fibres and the relationship of these sites to the protein composition of the Z disc.Proc. natn. Acad. Sci. U.S.A. 75, 3683–7.Google Scholar
  19. Maw, M. C. (1982)A-filaments: structure and reconstruction. Ph.D. thesis, University of Leicester, Leicester, U.K.Google Scholar
  20. Maw, M. C. &Rowe, A. J. (1980) Fraying of A-filaments into three subfilaments.Nature, Lond. 286, 412–4.Google Scholar
  21. Mihalyi, E. &Rowe, A. J. (1966) Studies on the extraction of actomyosin from rabbit muscle.Biochem. Z. 345, 267–85.Google Scholar
  22. Niederman, R. &Peters, L. K. (1982) Native bare zone assemblages nucleate myosin filament assembly.J. molec. Biol. 161, 505–17.Google Scholar
  23. Oosawa, F., Kasai, M., Hantano, S. &Asakura, S. (1966) InPrinciples of Biomolecular Organisation (edited byWolstenholme, G. E. W. andO'Connor, M.). Ciba Foundation Symposium, pp. 273–303. London: Churchill.Google Scholar
  24. Persechini, A. &Rowe, A. J. (1984) Modulation of myosin filament conformation by physiological levels of divalent cation.J. molec. Biol. 172, 23–39.Google Scholar
  25. Pinset-Harstrom, I. &Truffy, J. (1979) Effect of adenosine triphosphate, inorganic phosphate and divalent cations on the size and structure of synthetic myosin filaments. An electron microscopic study.J. molec. Biol. 134, 173–88.Google Scholar
  26. Reisler, E., Smith, C. &Seegan, G. (1980) Myosin minifilaments.J. molec. Biol. 143, 129–45.Google Scholar
  27. Reynold, E. S. (1963) The use of lead citrate at high pH as an electron-opaque stain in electron microscopy.J. Cell Biol. 17, 208–13.Google Scholar
  28. Rowe, A. J. &Maw M. C. (1984) InContractile Mechanisms in Muscle Contraction (edited byPollack, G. H. andSugi, H.), pp. 5–20. Seattle: Plenum.Google Scholar
  29. Spurr, A. R. (1969) A low-viscosity epoxy resin embedding medium for electron microscopy.J. Ultrastruct. Res. 26, 31–43.Google Scholar
  30. Tanaka, M. &Tanaka, H. (1979) Extraction and functional reformation of thick filaments in chemically skinned molluscan catch muscle fibres.J. Biochem. 85, 535–40.Google Scholar
  31. Taniguchi, M. &Ishikawa, H. (1982)In situ reconstitution of myosin filaments within the myosin-extracted myofibril in cultured skeletal muscle cells.J. Cell Biol. 92, 324–32.Google Scholar
  32. Tawada, K., Yoshida, A. &Morita, K. (1976) Myosin-free ghosts of single fibers and an attempt to re-form myosin filaments in the ghost fibers.J. Biochem. 80, 121–7.Google Scholar
  33. Trinick, J. A. (1973)A-filaments from rabbit skeletal muscle. Ph.D. Thesis, University of Leicester, Leicester, U.K.Google Scholar
  34. Trinick, J. A. &Cooper, J. (1981) Sequential disassembly of vertebrate skeletal muscle thick filaments.J. molec. Biol. 151, 309–14.Google Scholar
  35. Wang, K., McClure, J. &Tu, A. (1980) Titin: major myofibrillar components of striated muscle.Proc. natn. Acad. Sci. U.S.A. 76, 3698–702.Google Scholar
  36. Weisenberg, R. C. (1980) Role of co-operative interactions, microtubule-associated proteins and guanosine triphosphate in microtubule assembly: a model.J. molec. Biol. 139, 660–77.Google Scholar

Copyright information

© Chapman and Hall Ltd 1986

Authors and Affiliations

  • Maria C. Maw
    • 1
  • Arthur J. Rowe
    • 1
  1. 1.Department of Biochemistry, School of Biological SciencesUniversity of LeicesterLeicesterUK

Personalised recommendations