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Vol. 12, Issue 12, 3919-3932, December 2001
Department of Molecular, Cellular, and Developmental Biology,
University of Colorado, Boulder, Colorado 80309-0347
The kinesin superfamily of microtubule motor proteins is important
in many cellular processes, including mitosis and meiosis, vesicle
transport, and the establishment and maintenance of cell polarity. We
have characterized two related kinesins in fission yeast,
klp5+ and
klp6+, that are amino-terminal motors
of the KIP3 subfamily. Analysis of null mutants demonstrates that
neither klp5+ nor
klp6+, individually or together, is
essential for vegetative growth, although these mutants have altered
microtubule behavior. klp5
and klp6
are resistant to high concentrations of the microtubule poison
thiabendazole and have abnormally long cytoplasmic microtubules that
can curl around the ends of the cell. This phenotype is greatly enhanced in the cell cycle mutant cdc25-22, leading to
a bent, asymmetric cell morphology as cells elongate during cell cycle arrest. Klp5p-GFP and Klp6p-GFP both localize to cytoplasmic
microtubules throughout the cell cycle and to spindles in mitosis, but
their localizations are not interdependent. During the meiotic phase of
the life cycle, both of these kinesins are essential. Spore viability
is low in homozygous crosses of either null mutant. Heterozygous
crosses of klp5 with klp6 have an
intermediate viability, suggesting cooperation between these proteins
in meiosis.
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