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A more recent version of this article appeared on December 1, 2004
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Submitted on June 2, 2004
Revised on August 20, 2004
Accepted on September 8, 2004
*Institut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, 40225 Düsseldorf, Germany;
Biochemie-Zentrum Heidelberg, Ruprecht-Karls Universität, 69120 Heidelberg, Germany
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 extraSpc7, an essential kinetochore protein associated with the central centromere region. Mal3 and Spc7 interact physically as both proteins can be co-immunoprecipitated. Overexpression of a Spc7 variant severely compromises kinetochore-microtubule interaction indicating that the Spc7 protein plays a role in this process. Spc7 function appears to be conserved since, Spc105, a S. 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: fleigu{at}uni-duesseldorf.de