Biochemical and Cryo-EM studies of telomerase regulation
Telomeres are repeats of DNA bases that cap the ends of chromosomes, involved in protecting our genetic information. Telomerase is the enzyme responsible for maintaining telomere length – when activated, it adds repeats to telomere ends. Consequently, telomerase activity is implicated in aging and cancer, carrying important therapeutic implications. For the past year, I have been working with a postdoctoral fellow, Kelly Nguyen, in the Nogales Lab and Collins Lab to characterize the function and structure of shelterin, a protein complex involved in recruiting telomerase to the telomeres. In addition to employing negative staining and cryo-electron microscopy to study shelterin structure, we are using molecular and biochemical techniques such as molecular cloning, cell culture, and protein purification to build a more complete understanding of how shelterin interacts with telomerase.