All in all, we find that T. thermophila has a unique kinetochore combining both highly-divergent, but ancient, as well as more recently-evolved components into a functional whole. (10/11)

To uncover how the different components assemble in the T. thermophila kinetochore, we performed nanometer-scale intra-kinetochore measurements. This revealed that the T. thermophila kinetochore assembles much like the human kinetochore despite high levels of divergence. (7/11)

Using deep-homology searches with sequence-based methods as well as AlphaFold-based structural searches, we found a set of highly-diverse orthologs of known kinetochore components. Combined, these constitute a primary axis of the kinetochore: CENP-C, the MIS12 complex and the NDC80 complex. (4/11)

By performing proximity-labeling proteomics combined with microscopy on the few known kinetochore components in the classic model organism T. thermophila, we uncovered a range of proteins associated to its kinetochore, but it was unclear what the evolutionary origins of these proteins were. (3/11)

The kinetochore composition of ciliates has long been elusive, as they seemed to lack many known components. Moreover, they have a unique cell division process, as are binucleated but only one undergoes mitosis. We wanted to find out how they segregate their chromosomes during cell division. (2/11)