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PMID: 6583675 Published · ppublish English Journal Article

Interference of GTP hydrolysis in the mechanism of microtubule assembly: an experimental study.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 81 ·No. 3 ·1984-02-00 ·Pages 771-5

Carlier MF, Hill TL, Chen Y

Abstract

This paper reports an experimental study of the interference of GTP hydrolysis in the mechanism of microtubule assembly, following the model and theory previously published [Hill, T. L. & Carlier, M.-F. (1983) Proc. Natl. Acad. Sci. USA 80, 7234-7238]. Results from dilution experiments show that microtubules depolymerize faster below the critical concentration than expected with a reversible polymerization model. The experimental plot of flux versus tubulin concentration exhibits a slope discontinuity at the critical concentration, in agreement with the theory. Theoretical points calculated by the Monte Carlo method can be fitted qualitatively to the data. A consequence of this peculiar dynamic behavior of microtubules is that the ratio of tubulin dissociation and association rate constants measured, respectively, below and above the critical concentration does not yield the true value of the critical concentration. It is emphasized that the presence of GTP at microtubule ends is necessary to maintain the stability of the polymer.

MeSH Terms
Animals Guanosine Triphosphate/metabolism Hydrolysis Kinetics Macromolecular Substances Mathematics Microtubules/metabolism,ultrastructure Models, Biological Tubulin/metabolism
Chemicals
Macromolecular Substances Tubulin Guanosine Triphosphate
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Carlier M F
Hill T L
Chen Y
References (35)
35 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.81.3.771
Published
1984-02-00
Pages
771-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC344918
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.81.3.771 PMC Full Text View journal details
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