Reconstitution of a 26-subunit human kinetochore reveals cooperative 
microtubule binding by CENP-OPQUR and NDC80.

Pesenti, M. E.; Prumbaum, D.; Auckland, P.; Smith, C. M.; Faesen, A. C.; Petrovic, A.; Erent, M.; Maffini, S.; Pentakota, S.; Weir, J. R.; Lin, Y. C.; Raunser, S.; McAinsh, A. D.; Musacchio, A.

doi:10.1016/j.molcel.2018.07.038

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Reconstitution of a 26-subunit human kinetochore reveals cooperative microtubule binding by CENP-OPQUR and NDC80.

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Faesen, A. C.
Research Group Biochemistry of Signal Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

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Zitation

Pesenti, M. E., Prumbaum, D., Auckland, P., Smith, C. M., Faesen, A. C., Petrovic, A., et al. (2018). Reconstitution of a 26-subunit human kinetochore reveals cooperative microtubule binding by CENP-OPQUR and NDC80. Molecular Cell, 71(6), 923-939. doi:10.1016/j.molcel.2018.07.038.

Zitierlink: https://hdl.handle.net/21.11116/0000-0002-5569-9

Zusammenfassung

The approximately thirty core subunits of kinetochores assemble on centromeric chromatin containing the histone H3 variant CENP-A and connect chromosomes with spindle microtubules. The chromatin proximal 16-subunit CCAN (constitutive centromere associated network) creates a mechanically stable bridge between CENP-A and the kinetochore's microtubule-binding machinery, the 10-subunit KMN assembly. Here, we reconstituted a stoichiometric 11-subunit human CCAN core that forms when the CENP-OPQUR complex binds to a joint interface on the CENP-HIKM and CENP-LN complexes. The resulting CCAN particle is globular and connects KMN and CENP-A in a 26-subunit recombinant particle. The disordered, basic N-terminal tail of CENP-Q binds microtubules and promotes accurate chromosome alignment, cooperating with KMN in microtubule binding. The N-terminal basic tail of the NDC80 complex, the microtubule-binding subunit of KMN, can functionally replace the CENP-Q tail. Our work dissects the connectivity and architecture of CCAN and reveals unexpected functional similarities between CENP-OPQUR and the NDC80 complex.