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Title: Analysis of the proteins involved in chromosome cohesion in Drosophila melanogaster
Author: Vass, Sharron
Awarding Body: University of Edinburgh
Current Institution: University of Edinburgh
Date of Award: 2005
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The cohesin complex is primarily composed of two Structural Maintenance of Chromosomes proteins (SMC1 and SMC3), and two non-SMC subunits (rad2l/Sccl and SA1/Scc3). We have demonstrated that the Drosophila rad2l/Sccl homologue, Drad2l, is in a complex with SMC1, SMC3, and SA1/Scc3 and similar to other higher eukaryotes, the majority of Drad21-dissociates from chromosomes during prophase, although a small pool remains associated with centromeres until anaphase. In my work I have shown that the specific depletion of Drad21, by RNA interference in Drosophila S2 cells, results in a prometaphase delay, premature sister chromatid separation, and the selective destabilisation of SA1/Scc3. In addition, I also observed that the chromosome passenger protein INCENP becomes mis-localised in Drad21 depleted cells. As a collaborative aspect to this work I have been involved in the characterization of a number of Drad21 cleavage mutants. In S. cerevisiae the dissolution of sister chromatids is brought about by cleavage of scclp by a conserved cysteine protease Espl/Separase. Separase cleaves Sccl at a conserved site in budding and fission yeasts, humans and Xenopus. Although three potential cleavage sites have been identified in the Drosophila sequence, only one, gives rise to a phenotype when mutated. As a further project I have been working on a potential chromatin remodelling protein, which when deleted from S. pombe results in segregation defects and sensitivity to microtubule poisons. This protein has also been implicated in the correct targeting of rad2l to centromeric heterochromatin. This protein is conserved from yeast to mammals and I have been specifically characterizing the Drosophila homologue including a number of mutant alleles. Intriguingly, antibodies to this protein show a striking centromeric localization on mitotic chromosomes.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available