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Science 6 May 1994:
Vol. 264. no. 5160, pp. 839 - 842
DOI: 10.1126/science.8171338
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Articles

Science, Vol 264, Issue 5160, 839-842
Copyright © 1994 by American Association for the Advancement of Science

articles

Microtubule dynamics modulated by guanosine triphosphate hydrolysis activity of beta-tubulin

A Davis, CR Sage, CA Dougherty, and KW Farrell

Department of Biological Sciences, University of California, Santa Barbara 93106.

Microtubule dynamic instability underlies many cellular functions, including spindle morphogenesis and chromosome movement. The role of guanosine triphosphate (GTP) hydrolysis in dynamic instability was investigated by introduction of four mutations into yeast beta-tubulin at amino acids 103 to 109, a site thought to participate in GTP hydrolysis. Three of the mutations increased both the assembly-dependent rate of GTP hydrolysis and the average length of steady-state microtubules over time, a measure of dynamic instability. The fourth mutation did not substantially affect the rate of GTP hydrolysis or the steady-state microtubule lengths. These results demonstrate that the rate of GTP hydrolysis can modulate microtubule length and hence dynamic instability.


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Tubulin folding is altered by mutations in a putative GTP binding motif.
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Kinetochore motility after severing between sister centromeres using laser microsurgery: evidence that kinetochore directional instability and position is regulated by tension.
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Analysis of the gamma-tubulin sequences: implications for the functional properties of gamma-tubulin.
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