Abstract
THE interaction of actin and myosin which occurs during muscle contraction is regulated by changes in intracellular Ca2+ concentration. In vertebrates Ca2+ regulation is associated with troponin and tropomyosin in the thin filaments, and the myosin ATPase activity in the presence of pure actin is not Ca2+ sensitive. Most invertebrates possess a myosin-linked (thick filament) control system, usually in conjuction with actin-linked (thin filament) control1. Although the mechanism of thin filament regulation is fairly well characterised, that of thick filament control remains somewhat obscure (for reviews, see refs 2 and 3). This letter presents evidence for a structural and evolutionary relationship between proteins which have central roles in the two types of regulatory systems.
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
Lehman, W., and Szent-Györgyi, A. G., J. gen. Physiol., 66, 1–30 (1975).
Weber, A., and Murray, J. M., Physiol. Rev., 53, 612–673 (1973).
Szent-Györgyi, A. G., Biophys. J., 15, 707–723 (1975).
Weeds, A. G., Nature, 223, 1362–1364 (1969).
Weeds, A. G., and Lowey, S., J. molec. Biol., 61, 701–725 (1971).
Werber, M. M., Gaffin, S. L., and Oplatka, A., J. mechanochem. cell Motil., 1, 91–96 (1972).
Gaffin, S. L., and Oplatka, A., J. Biochem., 75, 277–281 (1974).
Werber, M. M., and Oplatka, A., Biochem. biophys. Res. Commun., 57, 823–830 (1974).
Huxley, H. E., Cold Spring Harb. Symp. quant. Biol., 37, 361–376 (1972).
Morimoto, K., and Harrington, W. F., J. molec. Biol., 88, 693–709 (1974).
Balint, M., Sreter, F. A., Wolf, I., Nagy, B., and Gergely, J., J. biol. Chem., 250, 6168–6177 (1975).
Potter, J. D., Fedn Proc., 34, 671 (1975).
Kendrick-Jones, J., Szentkiralyi, E. M., and Szent-Györgyi, A. G., Cold Spring Harb. Symp. quant. Biol., 37, 47–53 (1972).
Szent-Györgyi, A. G., Szentkiralyi, E. M., and Kendrick-Jones, J., J. molec. Biol., 74, 179–203 (1973).
Kendrick-Jones, J., Nature, 249, 631–634 (1974).
Collins, J. H., Potter, J. D., Horn, M. J., Wilshire, G., and Jackman, N., FEBS Lett., 36, 268–272 (1973); in Calcium Binding Proteins, (edit. by Drabikowski, W. Strzelecka-Golaszewska, H. and Carafoli, E.), 51–64 (Elsevier, Amsterdam, 1974).
Collins, J. H., Biochem. biophys. Res. Commun., 65, 604–610 (1975).
Collins, J. H., and Elzinga, M., J. biol. Chem., 250, 5906–5914 (1975).
Collins, J. H., Biochem. biophys. Res. Commun., 58, 301–308 (1974).
Weeds, A. G., and McLachlan, A. D., Nature, 252, 646–649 (1974).
Tufty, R. M., and Kretsinger, R. H., Science, 187, 167–169 (1975).
Barker, W. C., and Dayhoff, M. O., Biophys. J., 15, 121a (1975).
Kretsinger, R. H., and Barry, C. D., Biochim. biophys. Acta, 405, 40–52 (1975).
Pechère, J.-F., et al. in Calcium Transport in Secretion and Contraction (edit. by Carafoli, E. Clementi, F. Drabikowski, W. and Margreth, A.) (North Holland, Amsterdam, in the press).
Collins, J. H., in Calcium in Biological Systems (Cambridge University Press, in the press).
Kretsinger, R. H., and Nockolds, C. E., J. biol Chem., 248, 3313–3326 (1973).
Frank, G., and Weeds, A. G., Eur. J. Biochem., 44, 317–334 (1974).
Enfield, D. L., Ericson, L. H., Blum, H. E., Fischer, E. H., and Neurath, H., Proc. natn. A cad. Sci. U.S.A., 72, 1309–1313 (1975).
Perrie, W. T., Smillie, L. B., and Perry, S. V., Biochem. J., 135, 151–164 (1973).
Laki, K., J. cell. comp. Physiol., 49, 249–265 (1957).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
COLLINS, J. Homology of myosin DTNB light chain with alkali light chains, troponin C and parvalbumin. Nature 259, 699–700 (1976). https://doi.org/10.1038/259699a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/259699a0
This article is cited by
-
Immunocytochemically determined regulatory proteins, troponin, calponin and caldesmon, may occur together in the musculature of a Gordian worm (Ecdysozoa, Cycloneuralia, Nematomorpha)
Zoomorphology (2018)
-
Phosphorylation of the regulatory light chain of myosin in striated muscle: methodological perspectives
European Biophysics Journal (2016)
-
Drosophila melanogaster genes encoding three troponin-C isoforms and a calmodulin-related protein
Biochemical Genetics (1994)
-
Amino acid sequences of myosin essential and regulatory light chains from two clam species: Comparison with other molluscan myosin light chains
Journal of Muscle Research and Cell Motility (1991)
-
Myosin light chains and troponin C: Structural and evolutionary relationships revealed by amino acid sequence comparisons
Journal of Muscle Research and Cell Motility (1991)
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.
