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A more recent version of this article appeared on April 1, 2003
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Submitted on September 30, 2002
Revised on November 28, 2002
Accepted on December 26, 2002
1 Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853-2703, USA
2 Fox Chase Cancer Center, Philadelphia, PA 19111, USA
* Corresponding author. E-mail address: MLG11{at}cornell.edu.
The ZW10 and Rough Deal (ROD) proteins are part of a complex necessary for accurate chromosome segregation. This complex recruits cytoplasmic dynein to the kinetochore and participates in the spindle checkpoint. We used immunoaffinity chromatography and mass spectroscopy to identify the Drosophila proteins in this complex. We found that the complex contains an additional protein we name Zwilch. Zwilch localizes to kinetochores and kinetochore microtubules in a fashion identical to ZW10 and ROD. We have also isolated a zwilch mutant, which exhibits the same mitotic phenotypes associated with zw10 and rod mutations: lagging chromosomes at anaphase, and precocious sister chromatid separation upon activation of the spindle checkpoint. Zwilch's role within the context of this complex is evolutionarily conserved. The human Zwilch protein (hZwilch) co- immunoprecipitates with hZW10 and hROD from HeLa cell extracts, and localizes to the kinetochores at prometaphase. Finally, we discuss immunoaffinity chromatography results that suggest the existence of a weak interaction between the ZW10/ROD/Zwilch complex and the kinesin-like kinetochore component CENP-meta.
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