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Abstract:
Kinetochores are nucleoprotein assemblies responsible for the attachment
of chromosomes to spindle microtubules during mitosis. The KMN network,
a crucial constituent of the outer kinetochore, creates an interface
that connects microtubules to centromeric chromatin. The NDC80, MIS12,
and KNL1 complexes form the core of the KMN network. We recently
reported the structural organization of the human NDC80 complex. In this
study, we extend our analysis to the human MIS12 complex and show that
it has an elongated structure with a long axis of similar to 22 nm.
Through biochemical analysis, cross-linking-based methods, and
negative-stain electron microscopy, we investigated the reciprocal
organization of the subunits of the MIS12 complex and their contacts
with the rest of the KMN network. A highlight of our findings is the
identification of the NSL1 subunit as a scaffold supporting interactions
of the MIS12 complex with the NDC80 and KNL1 complexes. Our analysis has
important implications for understanding kinetochore organization in
different organisms.
