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Science 22 October 1999:
Vol. 286. no. 5440, pp. 782 - 785
DOI: 10.1126/science.286.5440.782

Reports

Microtubule Disassembly by ATP-Dependent Oligomerization of the AAA Enzyme Katanin

James J. Hartman, Ronald D. Vale *

Katanin, a member of the AAA adenosine triphosphatase (ATPase) superfamily, uses nucleotide hydrolysis energy to sever and disassemble microtubules. Many AAA enzymes disassemble stable protein-protein complexes, but their mechanisms are not well understood. A fluorescence resonance energy transfer assay demonstrated that the p60 subunit of katanin oligomerized in an adenosine triphosphate (ATP)- and microtubule-dependent manner. Oligomerization increased the affinity of katanin for microtubules and stimulated its ATPase activity. After hydrolysis of ATP, microtubule-bound katanin oligomers disassembled microtubules and then dissociated into free katanin monomers. Coupling a nucleotide-dependent oligomerization cycle to the disassembly of a target protein complex may be a general feature of ATP-hydrolyzing AAA domains.

The Howard Hughes Medical Institute and the Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA.
*   To whom correspondence should be addressed. E-mail: vale{at}phy.ucsf.edu


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