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Vol. 15, Issue 12, 5255-5267, December 2004
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* Institut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany;
Biochemie-Zentrum Heidelberg Ruprecht-Karls Universität, 69120 Heidelberg, Germany
Submitted June 2, 2004;
Revised August 20, 2004;
Accepted September 8, 2004
Monitoring Editor: Ted Salmon
A critical aspect of mitosis is the interaction of the kinetochore with spindle microtubules. Fission yeast Mal3 is a member of the EB1 family of microtubule plus-end binding proteins, which have been implicated in this process. However, the Mal3 interaction partner at the kinetochore had not been identified. Here, we show that the mal3 mutant phenotype can be suppressed by the presence of extra Spc7, an essential kinetochore protein associated with the central centromere region. Mal3 and Spc7 interact physically as both proteins can be coimmunoprecipitated. Overexpression of a Spc7 variant severely compromises kinetochoremicrotubule interaction, indicating that the Spc7 protein plays a role in this process. Spc7 function seems to be conserved because, Spc105, a Saccharomyces cerevisiae homolog of Spc7, identified by mass spectrometry as a component of the conserved Ndc80 complex, can rescue mal3 mutant strains.
Corresponding author. E-mail address: fleigu{at}uni-duesseldorf.de.
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