On the Possibility of Interaction between Neighbouring Crossbridges

  • R. T. Tregear
  • M. L. Clarke
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 37)


Demembranated insect or rabbit striated muscle fibres at equilibrium (i.e. in the absence of ATP hydrolysis) were modified either by substituting ethylene glycol for water or by adding AMPPNP. The resultant states observed by electron microscopy and X-ray diffraction appeared to contain a mixture of at least two distinct types of crossbridge, which were not randomly mixed. The crossbridges held tension for a great deal longer than they remained attached to actin in solution. In the presence of AMPPNP the muscle fibres relaxed at a critical glycol concentration. These properties indicate that the crossbridges interacted with one another.


Myosin Head Flight Muscle Layer Line Rabbit Muscle Contractile Mechanism 
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  1. Arata, T. and Podolsky, R.J. (1982). Crossbridge flexibility derived from the influence of lattice spacing on mechanical properties of muscles fibres in rigor. Biophys. J. 37: 362a.Google Scholar
  2. Barrington-Leigh, J., Goody, R.S., Holman, W., Holmes, K.C., Rosenbaum, G. and Tregear, R.T. (1977). In: Insect Flight Muscle ed. R.T. Tregear. Amsterdam: North-Holland pp 137–146.Google Scholar
  3. Clarke, M.L., Marston, S.B. and Tregear, R.T. (1980). An attempt to assess the biochemically effective actin concentration in rabbit skeletal muscle. J. Muscle Res. Cell. Motil. 1: 447–448.Google Scholar
  4. Clarke, M.L. (1982). The attachment of myosin heads to actin in the presence and absence of an unhydrolysable analogue of ATP. D. Phil. Thesis, Oxford.Google Scholar
  5. Clarke, M.L. and Tregear, R.T. (1982). Tension maintenance and crossbridge detachment. FEES Letters (in press).Google Scholar
  6. Ford, L.E., Huxley, A.F. and Simmons, R.M. (1981). The relation between stiffness and filament overlap in stimulated frog muscle fibres. J. Physiol. 311: 219–249.PubMedGoogle Scholar
  7. Goody, R.S., Barrington-Leigh, J., Mannherz, H.G., Tregear, R.T. and Rosenbaum, G. (1976). X-ray titration of binding of β, γ, imido ATP to myosin in insect flight muscle. Nature, 262: 613–615.PubMedCrossRefGoogle Scholar
  8. Holmes, K.C., Tregear, R.T. and Barrington-Leigh, J. (1980). Interpretation of the low angle X-ray diffraction from insect flight muscle in rigor. Proc. Roy. Soc. B. 207: 13–33.CrossRefGoogle Scholar
  9. Kuhn, H.J. (1973). Transformation of chemical energy into mechanical energy by glycerol-extracted fibres of insect flight muscle in the absence of nucleosidetriphosphate hydrolysis. Experientia, 29: 1086–1088.PubMedCrossRefGoogle Scholar
  10. Marston, S.B. (1973). Kinetic studies of the contractile mechanism of muscle. D. Phil. Thesis; University of Oxford.Google Scholar
  11. Marston, S.B. (1982). The rates of formation and dissociation of actin-myosin complexes. Biochem. J. 203: 453–480.PubMedGoogle Scholar
  12. Marston, S.B. and Weber, A.M. (1975). The dissociation constant of the actin-heavy meromyosin subfragment-1 complex. Biochemistry 14: 3868–3873.PubMedCrossRefGoogle Scholar
  13. Marston, S.B., Rodger, C.D. and Tregear, R.T. (1976). Changes in muscle crossbridges when β, γ - imido-ATP binds to myosin. J. Mol. Biol. 104: 263–276.PubMedCrossRefGoogle Scholar
  14. Marston, S.B., Tregear, R.T., Rodger, C.D. and Clarke, M.L. (1979). Coupling between the enzymatic site of myosin and the mechanical output of muscle. J. Mol. Biol. 128: 111–126.PubMedCrossRefGoogle Scholar
  15. Meisner, D. and Beinbrech, G. (1979). Alterations of crossbridge angle induced by β, γ-imido-adenosine-triphosphate. Electron microscope and optical diffraction studies on myofibrillar fragments of abdominal muscles of the crayfish Orconectes limosus. Eur. J. Cell. Biol. 19: 189–195.PubMedGoogle Scholar
  16. Miller A. and Tregear R.T. (1972). Structure of insect fibrillar flight muscle in the presence and absence of ATP. J. Mol. Biol. 70: 85–104.PubMedCrossRefGoogle Scholar
  17. Reedy, M.K. (1968). Ultrastructure of insect flight muscle. L screw sense and structural grouping in the rigor cross-bridge lattice. J. Mol. Biol. 31: 155–178.PubMedCrossRefGoogle Scholar
  18. Reedy, M.K., Leonard, K.R., Freeman, R and Arad, T. (1981). Thick myofilament mass determination by electron scattering measurements with the scanning transmission electron microscope. J. Musc. Res. Cell. Motil. 2: 45–64.CrossRefGoogle Scholar
  19. Reedy, M., Reedy, M.K. and Goody, R.S. (1981). Crossbridge structure in rigor and AMP.PNP states of insect flight muscle. Biophys. J. 33: 22a.Google Scholar
  20. Tregear, R.T., Milch, J., Goody, R.S., Holmes, K.C., and Rodger, C.D. (1979). X-ray diffraction of insect flight muscle. In: Crossbridge Mechanism in Muscle Contraction, pp 407–423, ed. by H. Sugi and G. Pollack, University of Tokyo Press.Google Scholar
  21. Tregear, R.T., Clarke, M.L., Marston, S.B., Rodger, C.D., Bordas, J., and Koch, M. (1982). A study of demembranated muscle fibres under equilibrium conditions. In: Basic Biology of Muscles: a Comparative Approach. Ed B. Twarog and R. Levine. Raven Press, NY..Google Scholar
  22. Wells, J.A., Sheldon, M. and Yount, R.G. (1980). Magnesium nucleotide is stoicheometrically trapped at the active site of myosin and its active proteolytic fragments by thíol cross-linking reagents. J. Biol. Chem. 255: 1598–1602.PubMedGoogle Scholar
  23. Williams, D.L. and Greene L.E. (1982). Comparison of the effect of tropomyosin and tropomin-tropomyosin on acto-51. Biophys. J. 37: 50a.Google Scholar

Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • R. T. Tregear
    • 1
  • M. L. Clarke
    • 2
  1. 1.ARC Institute of Animal PhysiologyBabraham, CambridgeUK
  2. 2.MRC Cell Biophysics UnitLondonUK

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