Green, Erin MJezek, Meagan2022-09-292022-09-292021-01-0112457http://hdl.handle.net/11603/25976Maintenance of telomeres, the transcriptionally silent nucleoprotein structures found at the ends of linear chromosomes, is necessary for genomic integrity. Altered telomere dynamics are associated with genomic instability and implicated in cellular aging and many types of cancer. Dysregulation of the chromatin structure at or adjacent to these protective caps can lead to dysfunctional telomeres. A number of proteins are involved in chromatin formation and maintenance. The enzyme Set1 is a lysine methyltransferase known to regulate chromatin dynamics through its modification of histone H3. Loss of Set1 is associated with defects in telomere silencing and maintenance, although the mechanism by which Set1 regulates telomeres is still unclear. The goal of this project was to further characterize the role Set1 plays at telomeres and elucidate the mechanisms underlying its functions in telomere silencing and maintenance. This has been done by assessing the catalytic and non-catalytic functions of Set1 at telomeres, and investigating its interactions with known telomere maintenance pathways. We have found that telomere maintenance by Set1 has H3K4 methylation dependent and independent components. We have also found that Set1-dependent telomere regulation is independent of the Sir complex, and instead likely dependent on regulation of CST (Cdc13-Stn1-Ten1) and telomerase by Set1. This information contributes to a more complete and comprehensive understanding of regulation of telomere integrity, which could play a vital role in the research into cellular aging and disease associated with abnormal gene regulation.application:pdfThis item may be protected under Title 17 of the U.S. Copyright Law. It is made available by UMBC for non-commercial research and education. For permission to publish or reproduce, please see http://aok.lib.umbc.edu/specoll/repro.php or contact Special Collections at speccoll(at)umbc.educhromatinH3K4 methylationSet1telomeresyeastInvestigation of the mechanism of Set1-mediated telomere silencing and maintenance in Saccharomyces cerevisiaeText