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Papers In Press, published online ahead of print June 16, 2005
J. Biol. Chem, 10.1074/jbc.M504070200
Submitted on April 14, 2005
Revised on May 31, 2005
Accepted on June 15, 2005
Department of Experimental Oncology, European Institute of Oncology, Milan I-20141
Corresponding Author: andrea.musacchio{at}ifom-ieo-campus.it
The Ndc80 complex is a constituent of the outer plate of the kinetochore and plays a critical role in establishing stable kinetochore-microtubule interactions required for chromosome segregation in mitosis. The Ndc80 complex is evolutionarily conserved and contains the four subunits Spc24, Spc25, Nuf2 and Ndc80 (whose human homologue is called Hec1). All four subunits are predicted to contain globular domains and extensive coiled-coils regions. To gain an insight into the organization of the human Ndc80 complex, we reconstituted it using recombinant methods. The hydrodynamic properties of the recombinant Ndc80 complex are identical to those of the endogenous HeLa cell complex and are consistent with a 1:1:1:1 stoichiometry of the four subunits and a very elongated shape. Two tight Hec1/Nuf2 and Spc24/Spc25 sub-complexes, each stabilized by a parallel heterodimeric coiled-coil, maintain this organization. These sub-complexes tetramerize via an interaction of the C- and N-terminal portions of the Hec1/Nuf2 and Spc24/Spc25 coiled-coils, respectively. The recombinant complex displays normal kinetochore localization upon injection in HeLa cells and is therefore a faithful copy of the endogenous Ndc80 complex.
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