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Vol. 12, Issue 10, 3161-3174, October 2001

-Tubulin and the C-Terminal Motor Domain Kinesin-like Protein, KLPA, Function in the Establishment of Spindle Bipolarity in Aspergillus nidulans

Natalie L. Prigozhina,^* Richard A. Walker, C. Elizabeth Oakley,^* and Berl R. Oakley^*§

 ^*Department of Molecular Genetics, Ohio State University, Columbus, Ohio 43210; and  Department of Biology, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061

Previous research has found that a -tubulin mutation in Schizosaccharomyces pombe is synthetically lethal with a deletion of the C-terminal motor domain kinesin-like protein gene pkl1, but the lethality of the double mutant prevents a phenotypic analysis of the synthetic interaction. We have investigated interactions between klpA1, a deletion of an Aspergillus nidulans homolog of pkl1, and mutations in the mipA, -tubulin gene. We find that klpA1 dramatically increases the cold sensitivity and slightly reduces the growth rate at all temperatures, of three mipA alleles. In synchronized cells we find that klpA1 causes a substantial but transient inhibition of the establishment of spindle bipolarity. At a restrictive temperature, mipAD123 causes a slight, transient inhibition of spindle bipolarity and a more significant inhibition of anaphase A. In the mipAD123/klpA1 strain, formation of bipolar spindles is more strongly inhibited than in the klpA1 single mutant and many spindles apparently never become bipolar. These results indicate, surprisingly, that -tubulin and the klpA kinesin have overlapping roles in the establishment of spindle bipolarity. We propose a model to account for these data.

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Present address: The Scripps Research Institute, Department of Cell Biology, MB-39, Room MBB201, 10550 North Torrey Pines Rd., La Jolla, CA 92037.

^§ Corresponding author. E-mail address: oakley.2{at}osu.edu.

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Molecular Biology of the Cell
Vol. 12, 3161-3174, October 2001
Copyright © 2001 by The American Society for Cell Biology

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