Determining the Individual Roles of Telomere-Associated Proteins in Telomere Regulation in Arabidopsis
Abstract
Telomeres consist of repeating sequences of nucleotides at the end of linear chromosomes and associated proteins that together serve to protect chromosome ends from degradation or fusion. Misregulation of telomeres leads to issues such as replication stress, DNA double-strand breaks, and other biological consequences that affect normal DNA replication and organismal viability. Telomerase—an essential enzyme for telomere function and maintenance—is responsible for telomere replication and the maintenance of telomere length. In Arabidopsis, studies have led to the discovery of a highly conserved and essential telomere protein complex CTC1/STN1/TEN1 (CST), which caps and protects the end of the chromosomes. The CTC1 and STN1 components of CST complex in Arabidopsis interact with telomere-associated proteins POT1a and TEN1, which positively and negatively regulate telomerase activity, respectively. This study will investigate how the individual telomere-associated proteins CTC1, STN1, TEN1, and POT1a interact with each other, with the telomere, and with telomerase in vivo. Mutations in amino acids important for mediating the physical interactions between these proteins will be introduced, and their effects on telomere regulation will be tested. Analyzing the biological consequences of these mutations, and their effect on telomere integrity, will give insight to the individual roles of telomere-associated proteins in vivo and advance understanding of how telomeres provide genome stability. As events caused by telomere dysfunction occur in a myriad of diseases related to defects in DNA and cell replication, the study of telomeres, specifically the CST complex, may provide insight into stem cell-related diseases and cancer.
Citation
Lessen, Gabrielle Marie (2018). Determining the Individual Roles of Telomere-Associated Proteins in Telomere Regulation in Arabidopsis. Undergraduate Research Scholars Program. Available electronically from https : / /hdl .handle .net /1969 .1 /164496.