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Guanosinetriphosphatase activity of tubulin associated with microtubule assembly.

Publication ,  Journal Article
David-Pfeuty, T; Erickson, HP; Pantaloni, D
Published in: Proc Natl Acad Sci U S A
December 1977

Tubulin, purified by cycles of assembly followed by phosphocellulose chromatography, exhibits a characteristic GTPase activity that is polymerization dependent and can be attributed to the tubulin itself. This activity has been observed, in a standard reassembly buffer containing low Mg2+, under three conditions that induce microtubule assembly: in the presence of microtubule-associated proteins, in the presence of DEAE-dextran, or after addition of high Mg2+ and glycerol. The phosphocellulose-purified tubulin showed no GTPase activity under the following nonpolymerizing conditions: in buffer with low Mg2+ in the absence of microtubule-associated proteins or DEAE-dextran, in buffer with high Mg2+ and glycerol at tubulin concentrations below the critical concentration, or when microtubule assembly was inhibited by vinblastine. Colchicine, on the other hand, while blocking microtubule assembly, induced a significant GTPase activity in the phosphocellulose-purified tubulin. During the process of assembly, GTP appears to be hydrolyzed as a free tubulin dimer polymerizes into a microtubule. A constant GTPase activity when polymerization equilibrium is reached apparently reflects the cyclic polymerization-depolymerization of tubulin dimers at the ends of the microtubules.

Duke Scholars

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

December 1977

Volume

74

Issue

12

Start / End Page

5372 / 5376

Location

United States

Related Subject Headings

  • Vinblastine
  • Tubulin
  • Swine
  • Phosphoric Monoester Hydrolases
  • Microtubules
  • Kinetics
  • Guanosine Triphosphate
  • Glycoproteins
  • GTP Phosphohydrolases
  • Colchicine
 

Citation

APA
Chicago
ICMJE
MLA
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David-Pfeuty, T., Erickson, H. P., & Pantaloni, D. (1977). Guanosinetriphosphatase activity of tubulin associated with microtubule assembly. Proc Natl Acad Sci U S A, 74(12), 5372–5376. https://doi.org/10.1073/pnas.74.12.5372
David-Pfeuty, T., H. P. Erickson, and D. Pantaloni. “Guanosinetriphosphatase activity of tubulin associated with microtubule assembly.Proc Natl Acad Sci U S A 74, no. 12 (December 1977): 5372–76. https://doi.org/10.1073/pnas.74.12.5372.
David-Pfeuty T, Erickson HP, Pantaloni D. Guanosinetriphosphatase activity of tubulin associated with microtubule assembly. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5372–6.
David-Pfeuty, T., et al. “Guanosinetriphosphatase activity of tubulin associated with microtubule assembly.Proc Natl Acad Sci U S A, vol. 74, no. 12, Dec. 1977, pp. 5372–76. Pubmed, doi:10.1073/pnas.74.12.5372.
David-Pfeuty T, Erickson HP, Pantaloni D. Guanosinetriphosphatase activity of tubulin associated with microtubule assembly. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5372–5376.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

December 1977

Volume

74

Issue

12

Start / End Page

5372 / 5376

Location

United States

Related Subject Headings

  • Vinblastine
  • Tubulin
  • Swine
  • Phosphoric Monoester Hydrolases
  • Microtubules
  • Kinetics
  • Guanosine Triphosphate
  • Glycoproteins
  • GTP Phosphohydrolases
  • Colchicine