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Science 20 August 1993:
Vol. 261. no. 5124, pp. 1044 - 1047
DOI: 10.1126/science.8102497

Articles

Science, Vol 261, Issue 5124, 1044-1047
Copyright © 1993 by American Association for the Advancement of Science


articles

Localization of an exchangeable GTP binding site at the plus end of microtubules

TJ Mitchison

Department of Pharmacology, University of California, San Francisco 94143-0450.

Microtubule polarity arises from the head-to-tail orientation of alpha-beta tubulin heterodimers in the microtubule lattice. The identity of the polypeptide at each end of the microtubule is unknown, but structural models predict that the beta-tubulin end contains an exchangeable guanosine triphosphate (GTP) binding site. When GTP-coated fluorescent beads were incubated with microtubules, they bound specifically to plus ends, suggesting that tubulin is oriented in microtubules with beta-tubulin toward the plus end.


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