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  <title><![CDATA[MS Defense by Tianyi Ye]]></title>
  <body><![CDATA[<p>In partial fulfillment of the requirements for the degree of</p><p>&nbsp;</p><p>Master of Science in Biology</p><p>in the</p><p>School of Biological Sciences</p><p>&nbsp;</p><p><strong>Tianyi Ye</strong></p><p><strong>&nbsp;</strong></p><p>Will defend his thesis</p><p>&nbsp;</p><p><strong>“Functional Roles of Rad52 and RPA in Inverse RNA Strand Exchange”</strong></p><p><strong>&nbsp;</strong></p><p>22, April, 2026</p><p>10: 00 AM (EST) in EBB-1-5024.</p><p><a href="https://nam12.safelinks.protection.outlook.com/?url=https%3A%2F%2Fgatech.zoom.us%2Fj%2F92351872480%3Fpwd%3D5Yq8gGcTDl5HY45siEZe6qIpwpUj8w.1&amp;data=05%7C02%7Ctm186%40gtvault.onmicrosoft.com%7C0c938265c47741cfa51908de99617496%7C482198bbae7b4b258b7a6d7f32faa083%7C1%7C0%7C639116841029702073%7CUnknown%7CTWFpbGZsb3d8eyJFbXB0eU1hcGkiOnRydWUsIlYiOiIwLjAuMDAwMCIsIlAiOiJXaW4zMiIsIkFOIjoiTWFpbCIsIldUIjoyfQ%3D%3D%7C0%7C%7C%7C&amp;sdata=cWMBF3MSJkdBetWH3V9KFElL416LKPvZBSVOR7sdlGg%3D&amp;reserved=0">https://gatech.zoom.us/j/92351872480?pwd=5Yq8gGcTDl5HY45siEZe6qIpwpUj8w.1</a></p><p>&nbsp;</p><p>&nbsp;</p><p>Passcode: <em>[To be shared on the day of]</em></p><p><strong>&nbsp;</strong></p><p><strong>Thesis Advisor:</strong></p><p>Dr. Francesca Storici</p><p>School of Biological Sciences</p><p>Georgia Institute of Technology</p><p>&nbsp;</p><p><strong>Committee Members:</strong></p><p>Dr. Yury O. Chernoff</p><p>School of Biological Sciences</p><p>Georgia Institute of Technology</p><p>&nbsp;</p><p><strong>&nbsp;</strong>Dr. Alexander Mazin</p><p>Department of Biochemistry and Structural Biology</p><p>UT Health San Antonio</p><p>&nbsp;&nbsp;</p><p><strong>Abstract:&nbsp;</strong>RNA-templated DNA repair has emerged as an alternative pathway for maintaining genome stability following DNA double-strand breaks (DSBs). Rad52 is a key factor in homologous recombination (HR), where it promotes strand annealing and coordinates repair intermediates. Previous in vitro studies have shown that interaction between Rad52 and replication protein A (RPA) influences inverse RNA strand exchange, a reaction in which RNA can guide DNA repair. These findings suggest a role for Rad52–RPA interaction in RNA-templated DNA repair; however, whether this mechanism operates in vivo remains unclear.</p><p>In this study, we developed a yeast-based system to investigate the role of Rad52–RPA interaction in RNA-templated DNA repair. Using a chromosomal reporter assay in which restoration of gene function serves as a quantitative readout, we measured repair frequency as a proxy for inverse RNA strand exchange and evaluated Rad52 variants with disrupted RPA interaction. This approach enables direct assessment of the requirement for Rad52–RPA interaction in RNA-dependent repair in vivo and provides new insight into RNA-mediated DNA repair mechanisms.</p>]]></body>
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