Roles of Nucleoside Triphosphates in Microtubule Assembly
- 1 June 1976
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 79 (6) , 1357-1364
- https://doi.org/10.1093/oxfordjournals.jbchem.a131190
Abstract
Depolymerization of microtubules in the ATP-reassembly buffer permitted the preparation of GDPETNGTP. Incubation of this tubulin fraction at 35° with ATP induced the phosphorylation of E-site GDP into GTP, which was then dephosphorylated during microtubule assembly. Incubation of GDPETNGTP with phosphoenolpyruvate and pyruvate kinase [EC 2, 7.1.40] also induced polymerization. Depolymerization of microtubules in the GTP-reassembly buffer yielded GTPETNGTP, which was capable of polymerizing into microtubules even in the absence of free GTP. In the presence of 4 M glycerol, GDPETNGTP assembled into microtubules with no change in the bound nucleotides.Keywords
This publication has 5 references indexed in Scilit:
- Polymerization of actin free from nucleotide and divalent cationsBiochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1965
- A simple method for the preparation of 32P-labelled adenosine triphosphate of high specific activityBiochemical Journal, 1964
- Measurement of the incorporation of radioactive amino acids into protein by a filter-paper disk methodArchives of Biochemistry and Biophysics, 1961
- Isolation, detection and measure of microgram quantities of labeled tissue nucleotidesArchives of Biochemistry and Biophysics, 1959
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951