Steady-state theory of the interference of GTP hydrolysis in the mechanism of microtubule assembly.
- 1 December 1983
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 80 (23), 7234-7238
- https://doi.org/10.1073/pnas.80.23.7234
Abstract
A model is presented for the interference of GTP hydrolysis in the mechanism of microtubule assembly. This model is suggested by previous results showing that both GTP and GDP are present at microtubule ends because of GTP hydrolysis and that tubulin does not bind to a GDP-bound end. The analytical theory developed here is aimed at calculation of the steady-state subunit flux at one end of the polymer. The GTP/GDP features just mentioned result in a nonlinear plot of the flux vs. tubulin concentration. Microtubules are predicted to exhibit a differen kinetic behavior below and avove the critical concentration, which can be considered as a transition between 2 regimes.Keywords
This publication has 8 references indexed in Scilit:
- Guanosine-5?-triphosphate hydrolysis and tubulin polymerizationMolecular and Cellular Biochemistry, 1982
- Mechanism of K+-induced actin assembly.The Journal of cell biology, 1982
- Assembly of microtubule protein: role of guanosine di- and triphosphate nucleotidesBiochemistry, 1982
- Bioenergetics and Kinetics of Microtubule and Actin Filament Assembly–DisassemblyInternational Review of Cytology, 1982
- Kinetic analysis of guanosine 5'-triphosphate hydrolysis associated with tubulin polymerizationBiochemistry, 1981
- Guanosinetriphosphatase activity of tubulin associated with microtubule assembly.Proceedings of the National Academy of Sciences, 1977
- Head to tail polymerization of actinJournal of Molecular Biology, 1976
- Tubulin-nucleotide interactions during the polymerization and depolymerization of microtubulesBiochemistry, 1976