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Vol. 11, Issue 12, 4067-4077, December 2000
Department of Biology, New York University, New York, New York
10003-6688
Moe1 is a conserved fission yeast protein that negatively affects
microtubule stability/assembly. We conducted a two-hybrid screen to
search for Moe1-binding proteins and isolated Mal3, a homologue of
human EB1. We show that Moe1 and Mal3 expressed in bacteria form a
complex and that Moe1 and Mal3 expressed in fission yeast cosediment
with microtubules. Deletion of either moe1 or
mal3 does not result in lethality; however, deletion of both moe1 and mal3 leads to cell death in
the cold. The resulting cells appear to die of chromosome
missegregation, which correlates with the presence of abnormal
spindles. We investigated the cause for the formation of monopolar
spindles and found that only one of the two spindle pole bodies (SPBs)
contains 
-tubulin, although both SPBs appear to be equal in size and
properly inserted in the nuclear membrane. Moreover, the moe1
mal3 double null mutant in the cold contains abnormally short
and abundant interphase microtubule bundles. These data suggest that
Moe1 and Mal3 play a role in maintaining proper microtubule
dynamics/integrity and distribution of -tubulin to the SPBs during
mitosis. Finally, we show that human Moe1 and EB1 can each rescue the
phenotype of the moe1 mal3 double null mutant and form a
complex, suggesting that these proteins are part of a well-conserved
mechanism for regulating spindle functioning.
Corresponding author. E-mail address:
eric.chang{at}nyu.edu.
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