User:Iannaa/Monopolin

Article Draft
Monopolin is a protein complex that in budding yeast is composed of the four proteins CSM1, HRR25, LRS4, and MAM1. Monopolin is required for the segregation of homologous centromeres to opposite poles of a dividing cell during anaphase I of meiosis. This occurs by bridging DSN1 kinetochore proteins to sister kinetochores within the centromere to physically fuse them and allow for the microtubules to pull each homolog toward opposite mitotic spindles.

Molecular strucure
Monopolin is composed of a 4 CSM1:2 LRS4 complex which forms a V-shaped structure with two globular heads at the ends. Bound to each CSM1 head is a MAM1 protein which recruits one copy of the HRR25 kinase. The hydrophobic cavity on the CSM1 subunit allows the hydrophobic regions of Monopolin receptor and kinetochore protein DSN1 to bind and furthermore directly crosslink sister kinetochores.