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Vol. 12, Issue 12, 4000-4012, December 2001

Department of Genetics, Section of Molecular and Cellular Biology,
University of California, Davis, California 95616
NOD is a Drosophila chromosome-associated
kinesin-like protein that does not fall into the chromokinesin
subfamily. Although NOD lacks residues known to be critical for kinesin
function, we show that microtubules activate the ATPase activity of NOD >2000-fold. Biochemical and genetic analysis of two genetically identified mutations of NOD (NODDTW and
NOD"DR2") demonstrates that this allosteric activation
is critical for the function of NOD in vivo. However, several lines of
evidence indicate that this ATPase activity is not coupled to vectorial
transport, including 1) NOD does not produce microtubule gliding; and
2) the substitution of a single amino acid in the
Drosophila kinesin heavy chain with the analogous amino
acid in NOD results in a drastic inhibition of motility. We suggest
that the microtubule-activated ATPase activity of NOD provides
transient attachments of chromosomes to microtubules rather than
producing vectorial transport.
Stowers Institute for Medical Research, 1000 E. 50th St.,
Kansas City, MO 64110, E-mail address: RSH{at}Stowers-Institute.org.
Corresponding author. E-mail address:
RSH{at}Stowers-Institute.org.
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