Non-claret disjunctional (Ncd) is a Drosophila kinesin-like motor required
for spindle assembly and maintenance in oocytes and early embryos. Ncd has
an ATP-independent microtubule binding site in the N-terminal tail domain a
s well as an ATP-dependent microtubule binding site in the C-terminal motor
domain. The Ncd tail domain shares many properties with the microtubule-as
sociated proteins that regulate microtubule assembly, including microtubule
binding and bundling activity and an abundance of basic and proline residu
es. Given these similarities, we examined the ability of Ncd tail domain pr
oteins to promote MT assembly and stability. The results indicate that the
Ncd tail domain can promote MT assembly and stabilize MTs against condition
s that induce MT disassembly, and suggest that Ncd may influence MT dynamic
s within the spindle. (C) 1999 Academic Press.