Abstract
The topography of the rigor complex between F-actin and myosin heads (S1) has been investigated by carbodiimide zero-length cross-linking. The results demonstrate for the first time that the 95,000-molecular weight (95K) heavy chain of the myosin head enters into van der Waals contact with two neighbouring actin monomers; one is bound to the 50K domain and the other to the 20K domain of the myosin chain. The covalent F-actin–S1 complex can be isolated; it shows a vastly elevated Mg2+-ATPase. Each pair of actin subunits in the thin filament seems to act as a functional unit for specific binding of a myosin head and stimulation of its Mg2+-ATPase activity.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Weeds, A. G. & Taylor, R. S. Nature 257, 54–56 (1975).
Mornet, D., Pantel, P., Audemard, E. & Kassab, R. Biochem. biophys. Res. Commun. 89, 925–932 (1979).
Mornet, D., Bertrand, R., Pantel, P., Audemard, E. & Kassab, R. Biochemistry 20, 2110–2120(1981).
Mornet, D., Pantel, P., Bertrand, R., Audemard, E. & Kassab, R. FEES Lett. 123, 54–58 (1981).
Gallagher, M. & Elzinga, M. Fedn Proc. 39, 2168 (1980).
Bárány, M. & Bárány, K. Biochim. biophys. Acta 41, 204–216 (1960).
White, H. D. & Taylor, E. W. Biochemistry 15, 5818–5826 (1976).
Margossian, S. S. & Lowey, S. J. molec. Biol. 74, 313–330 (1973).
Lovell, S. J. & Harrington, W. F. Fedn Proc. 39, 1935 (1980).
Marston, S. B., Tregear, R. T., Rodger, C. D. & Clarke, M. L. J. molec. Biol. 128, 111–126 (1979).
Namba, K., Wakabayashi, K. & Mitsui, T. J. molec. Biol. 138, 1–26 (1980).
Craig, R. et al. J. molec. Biol. 140, 35–55 (1980).
Taylor, E. W., CRC crit. Rev. Biochem. 6, 103–164 (1979).
Stein, L. A., Schwarz, R. P., Chock, P. B. & Eisenberg, E. Biochemistry 18, 3895–3909 (1979).
Bárány, M. & Burt, C. T., Fedn Proc. 38, 338 (1979).
Estes, E. J. & Gershman, L. C. Biochemistry 17, 2495–2499 (1978).
Fasold, H., Baumert, H. & Bender, N.,Biochem. Soc. Trans. 3, 935–936 (1975).
Spudich, J. A. & Watt, S. J. biol. Chem. 246, 4866–4871 (1971).
Takashi, R. Biochemistry 18, 5164–5169 (1979).
Duke, J., Takashi, R., Ue, K. & Morales, M. F. Proc. natn. Acad. Sci. U.S.A. 73, 302–306 (1976).
Mornet, D., Pantel, P., Audemard, E. & Kassab, R. Eur. J. Biochem. 100, 421–431 (1979).
Cooke, R. & Franks, K. Biochemistry 19, 2265–2269 (1980).
Takashi, R., Duke, J., Ue, K. & Morales, M. F. Archs Biochem. Biophys. 175, 279–283 (1976).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Mornet, D., Bertrand, R., Pantel, P. et al. Structure of the actin–myosin interface. Nature 292, 301–306 (1981). https://doi.org/10.1038/292301a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/292301a0
This article is cited by
-
The path to visualization of walking myosin V by high-speed atomic force microscopy
Biophysical Reviews (2014)
-
Fabrication of semiconductor nanowires by conjugation of quantum dots to actin filaments
Analytical and Bioanalytical Chemistry (2009)
-
The “Steric blocking model”, the “six-state model”, and the ATPase activity of regulated actomyosin
Cell Biophysics (1995)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
