Abstract
MICROTUBULE assembly in vitro requires (in normal conditions) that GTP be bound to the exchangeable nucleotide-binding site of tubulin1–3. The bound GTP is hydrolysed during polymerisation and the resulting GDP remains bound to the microtubule while the phosphate is released into the medium. Although hydrolysis normally occurs during polymerisation, microtubules will form in a non-hydrolysable analogue of GTP, guanylyl imidodiphosphate (GMP-PNP)4–6. We have observed6, as also has Arai5, that microtubules polymerised in GMP-PNP are not depolymerised by concentrations of Ca which completely depolymerise GTP microtubules. We have now found that GMP-PNP microtubules do not display evidence for a rapid equilibrium between polymer and subunit. The irreversible behaviour of GMP-PNP microtubules may explain the insensitivity to Ca and suggests a function for nucleotide hydrolysis during tubulin polymerisation.
Similar content being viewed by others
References
Weisenberg, R. C., Science, 177, 1104–1105 (1972).
Jacobs, M., Smith, H., and Taylor, E. W., J. molec. Biol., 89, 455–468 (1974).
Kobayashi, T., J. Biochem., 77, 1193–1197 (1975).
Lockwood, A. H., Penningroth, S. M., and Kirschner, M. W., Fedn. Proc., 34, 540 (1975).
Arai, T., and Kaziro, Y., Biochem, biophys. Res. Commun., 69, 369–376 (1976).
Weisenherg, R. C., Deery, W. J., and Dickinson, P., Biochemistry (in the press).
Gaskin, F., Cantor, C. R., and Shelanski, M. L., J. molec. Biol., 89, 737–738 (1976).
Olmsted, J. B., Marcum, J. M., Johnson, K. A., and Borisy, G. G., J. supramolec. Struct., 2, 429–450 (1974).
Engelborghs, Y., Heremans, K. A. H., DeMaeyer, L. C. M., and Hoebeke, J., Nature, 259, 686–688 (1976).
Oosawa, F., and Kasai, M., J. molec. Biol., 4, 10–21 (1962).
Cooke, R., Biochemistry, 14, 3250–3256 (1975).
Bender, N., Fasold, H., and Rack, M., FEBS Lett., 44, 209–212 (1974).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
WEISENBERG, R., DEERY, W. Role of nucleotide hydrolysis in microtubule assembly. Nature 263, 792–793 (1976). https://doi.org/10.1038/263792a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/263792a0
- Springer Nature Limited
This article is cited by
-
Mechanism of microtubule stabilization by taccalonolide AJ
Nature Communications (2017)
-
Mechanisms of developmental neurite pruning
Cellular and Molecular Life Sciences (2015)
-
Control of spindle form and function in grasshopper spermatocytes
Chromosoma (1978)