Slx8 Facilitates Loading of Rad51 at CAG Repeats in Saccharomyces cerevisiae
AbiChedid, Anicka
2023
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Repetitive DNA sequences in the genome have been shown to form alternative DNA structures and have been implicated in a variety of genetic diseases. The CAG trinucleotide repeat can form imperfect hairpin and slipped-strand structures, which is detrimental to DNA replication since the replisome has difficulty passing these barriers. Changes in the number of repeats within this region can occur ... read moreduring repair. Most notably, expansions in CAG repeat number are the cause of neurodegenerative diseases, like Huntington’s disease and spinocerebellar ataxia, when they occur in the implicated gene. It has been previously shown that expanded CAG repeats relocate from the interior of the nucleus to the nuclear pore complex (NPC) for repair. The type of repair happening at the NPC is especially interesting to study since genome integrity is preserved and changes in repeat number are less likely to occur here. Movement of the repeats to the NPC is in part dependent on the SUMOylation state of other DNA repair proteins, and the Slx5-Slx8 complex plays an active role in regulating this movement. Interestingly, the Rad51 recombinase has been shown to load at the CAG repeats only after they relocate to the NPC. In this study, we assess the roles of three proteins, Slx8, Srs2, and Sgs1, in relation to the loading of Rad51 at CAG repeats. We used fluorescence microscopy to measure the colocalization instances of the Rad51 protein with the CAG repeat locus in the absence of each of these proteins. The results of these experiments suggest that Slx8 regulates Rad51 loading both before and after the CAG repeats relocate to the nuclear pores.
Thesis (B.S.)--Tufts University, 2023.
Submitted to the Dept. of Biology.
Advisor: Catherine Freudenreich.read less - ID:
- 7s75dt64t
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