Understanding the mechanism of cohesion establishment (360G-Wellcome-097297_Z_11_Z)

The cohesin ring topologically entraps sister chromatids to ensure timely and error-free chromosome segregation during cell division. In interphase, cohesin is continually loaded onto and removed from the DNA by kollerin and releasin complexes, respectively. Acetylation of the ring is crucial for cohesion establishment this modification is believed to overpower the antiestablishment activity of releasin. In many systems outside of yeast, another essential protein sororin is also required for releasin neutralisation. One of the minor aims of this project is to conduct a small-scale screen to determine whether or not sororin exists in Saccharomyces cerevisiae. The primary goal of this project is to investigate the anti-establishment activity of releasin. One of the key aims is to determine whether releasin has the ability to physicallyremove cohesin from both DNA strands. The bulk of this project will involve reconstituting releasin activity in vitro by building on an existing physical assay for cohesion. Ultimately, this project aims to establish the minimal requirements for the anti-establishment activity of releasin.