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γ-Tubulin and the C-terminal motor domain kinesin-like protein, KLPA, function in the establishment of spindle bipolarity in Aspergillus nidulans
Prigozhina, Natalie L. Walker, Richard A. Oakley, C. Elizabeth Oakley, Berl R.
Prigozhina, Natalie L.
Walker, Richard A.
Oakley, C. Elizabeth
Oakley, Berl R.
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Abstract
Previous research has found that a γ-tubulin mutation inSchizosaccharomyces pombe is synthetically lethal with a deletion of the C-terminal motor domain kinesin-like protein genepkl1, 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, γ-tubulin gene. We find that klpA1 dramatically increases the cold sensitivity and slightly reduces the growth rate at all temperatures, of threemipA alleles. In synchronized cells we find thatklpA1 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 theklpA1 single mutant and many spindles apparently never become bipolar. These results indicate, surprisingly, that γ-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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2001-10-01
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American Society for Cell Biology
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Prigozhina, N., Walker, R., Oakley, C., & Oakley, B. (2001). γ-Tubulin and the C-terminal motor domain kinesin-like protein, KLPA, function in the establishment of spindle bipolarity in Aspergillus nidulans. Molecular Biology of the Cell, 12(10), 3161-3174. http://www.dx.doi.org/10.1091/mbc.12.10.3161