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A more recent version of this article appeared on June 1, 2002
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Submitted on September 20, 2001
Revised on February 7, 2002
Accepted on February 25, 2002
1 Dept. of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853-2703 (present address: Genomics Institute of the Novartis Research Foundation, 3115 Merryfield Row, Suite 200, San Diego, CA 92121-1125)
2 Dept. of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853-2703
* Corresponding author. E-mail address: tch4{at}cornell.edu.
Formation of the bipolar mitotic spindle relies on a balance of forces acting on the spindle poles. The primary outward force is generated by the kinesin-related proteins of the bim C family that cross-link antiparallel interpolar microtubules and slide them past each other. Here we provide evidence that Stu1p is also required for the production of this outward force in the yeast, S. cerevisiae. In the temperature-sensitive stu1-5 mutant, spindle pole separation is inhibited and preanaphase spindles collapse with their previously separated poles being drawn together. The temperature-sensitivity of stu1-5 can be suppressed by doubling the dosage of Cin8p, a yeast Bim C kinesin-related protein. Stu1p was observed to be a component of the mitotic spindle localizing to the midregion of anaphase spindles. It also binds to microtubules in vitro and we have examined the nature of this interaction. We show that Stu1p interacts specifically with ß-tubulin and identify the domains required for this interaction on both Stu1p and ß-tubulin. Taken together, these findings suggest that Stu1p binds to interpolar microtubules of the mitotic spindle and plays an essential role in their ability to provide an outward force on the spindle poles.
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