Nucleotide specificity in microtubule assembly in vitro
- 21 February 1978
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 17 (4), 734-740
- https://doi.org/10.1021/bi00597a028
Abstract
A procedure is described for removing most of the GDP bound at the exchangeable GTP binding site (E site) of tubulin. Microtuble protein [porcine brain] containing substoichiometric amounts of GDP at the E site is found to polymerize in response to: 2 nonhydrolyzable ATP analogs, adenylyl imidodiphosphate and adenylyl .beta.,.gamma.-methylenediphosphonate, and substoichiometric levels of GTP or dGTP. The results suggest that when GDP is removed from tubulin, the E site shows broad specificity for nucleoside triphosphates, and that microtubule assembly can be induced by the binding of substoichiometric amounts of nucleoside triphosphate to the E site.This publication has 8 references indexed in Scilit:
- Nucleotide binding and phosphorylation in microtubule assembly in vitroJournal of Molecular Biology, 1977
- Neurotubule assembly at substoichiometric nucleotide levels using a GTP regenerating systemBiochemical and Biophysical Research Communications, 1977
- Removal of a bound ligand from a macromolecule by gel filtrationBiochemical Journal, 1976
- Tubulin-nucleotide interactions during the polymerization and depolymerization of microtubulesBiochemistry, 1976
- Roles of Nucleoside Triphosphates in Microtubule AssemblyThe Journal of Biochemistry, 1976
- Effect of guanine nucleotides on the assembly of brain microtubules: Ability of 5′-guanylyl imidodiphosphate to replace GTP in promoting the polymerization of microtubules in vitroBiochemical and Biophysical Research Communications, 1976
- ISOLATION OF A PROTEIN SUBUNIT FROM MICROTUBULESThe Journal of cell biology, 1967
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951