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