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Updated: May 2, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
The kinetochore protein Moa1 enables cohesion-mediated monopolar attachment at meiosis I
Shihori Yokobayashi1, Yoshinori Watanabe
1Laboratory of Chromosome Dynamics, Institute of Molecular and Cellular Biosciences, Graduate Program in Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, SORST, Japan Science and Technology Agency, Yayoi, Tokyo 113-0032, Japan.
Abstract:
Meiosis resembles mitosis but employs a unique "reductional" nuclear division to allow the production of haploid gametes from diploid cells. The crucial ploidy reduction step requires that sister kinetochores attach to microtubules emanating from the same spindle pole, achieving "monopolar attachment," which ensures that maternal and paternal chromosomes are segregated. Here we screened for factors required to establish monopolar attachment in fission yeast and identified a novel protein, Moa1. Moa1 is meiosis specific and localizes exclusively to the central core of the centromere, a region that binds meiotic Rec8-containing cohesin complexes but not mitotic Rad21/Scc1-containing complexes. Enforced cleavage of Rec8 in the central core region led to the disruption of monopolar attachment, as in moa1Delta cells, without diminishing Moa1 localization. Moa1 physically interacts with Rec8, implying that Moa1 functions only through Rec8, presumably to facilitate central core cohesion. These results prove that monoorientation of kinetochores is established in a cohesion-mediated manner.
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