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LOCALIZATION OF AN EXCHANGEABLE GTP-BINDING SITE AT THE PLUS END OF MICROTUBULES
Author(s): MITCHISON TJ
Source: SCIENCE    Volume: 261    Issue: 5124    Pages: 1044-1047    Published: AUG 20 1993  
Times Cited: 93     References: 18     
Abstract: Microtubule polarity arises from the head-to-tall 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.
Document Type: Article
Language: English
Reprint Address: MITCHISON, TJ (reprint author), UNIV CALIF SAN FRANCISCO, DEPT PHARMACOL, SAN FRANCISCO, CA 94143 USA
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005
Subject Category: Multidisciplinary Sciences
IDS Number: LT747
ISSN: 0036-8075
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