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Journal Article

The COMA complex interacts with Cse4 and positions Sli15/Ipl1 at the budding yeast inner kinetochore

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Rojas,  Julie
Zachariae, Wolfgang / Chromosome Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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elife-42879-v2.pdf
(Publisher version), 6MB

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elife-42879-figures-v2.pdf
(Supplementary material), 9MB

Citation

Fischboeck-Halwachs, J., Singh, S., Potocnjak, M., Hagemann, G., Solis-Mezarino, V., Woike, S., et al. (2019). The COMA complex interacts with Cse4 and positions Sli15/Ipl1 at the budding yeast inner kinetochore. eLife, 8: e42879. doi:10.7554/eLife.42879.


Cite as: https://hdl.handle.net/21.11116/0000-0003-E787-0
Abstract
Kinetochores are macromolecular protein complexes at centromeres that ensure accurate chromosome segregation by attaching chromosomes to spindle microtubules and integrating safeguard mechanisms. The inner kinetochore is assembled on CENP-A nucleosomes and has been implicated in establishing a kinetochore-associated pool of Aurora B kinase, a chromosomal passenger complex (CPC) subunit, which is essential for chromosome biorientation. By performing crosslink-guided in vitro reconstitution of budding yeast kinetochore complexes we showed that the Ame1/Okp1(CENP-U/Q) heterodimer, which forms the COMA complex with Ctf19/Mcm21(CENP-P/O), selectively bound Cse4(CENP-A) nucleosomes through the Cse4 N-terminus. The Sli15/Ipl1(INCENP/Aurora-B) core-CPC interacted with COMA in vitro through the Ctf19 C-terminus whose deletion affected chromosome segregation fidelity in Sli15 wild-type cells. Tethering Sli15 to Ame1/Okp1 rescued synthetic lethality upon Ctf19 depletion in a Sli15 centromere-targeting deficient mutant. This study shows molecular characteristics of the point-centromere kinetochore architecture and suggests a role for the Ctf19 C-terminus in mediating CPC-binding and accurate chromosome segregation.