Poster abstracts
Poster number 21 submitted by Justin Davis
Insights into RNA-protein interactions in Trypanosoma brucei telomerase
Justin A. Davis (University of North Carolina at Charlotte ), Kausik Chakrabarti (University of North Carolina at Charlotte )
Abstract:
Telomeres are the nucleoprotein structures found at the end of eukaryotic linear chromosomes. Because conventional DNA polymerases are unable to fully replicate the ends of linear chromosomes, the activity of the ribonucleoprotein enzyme telomerase is required to counteract the progressive loss of DNA after every cell division. The telomerase enzyme consists of two main components: the telomerase reverse transcriptase (TERT) protein and the telomerase RNA (TR), which provides the template for telomeric DNA synthesis. The TR forms a large structural scaffold on which accessory proteins can bind in order to form the complete telomerase holoenzyme in vivo. These accessory proteins are required for proper telomerase activity and regulation inside of cells. Interacting partners of TERT have been extensively characterized in yeast, human, and Tetrahymena systems. These interactors have not been extensively studied in lower eukaryotes including clinically relevant human parasites like Trypanosoma brucei (T. brucei), a causative agent of African sleeping sickness in humans. These parasites require constant telomerase activity in order to rapidly divide in their host and establish a chronic infection. In this study, we determined the telomerase interactome of the bloodstream forms of T. brucei by immunoaffinity purification and mass spectrometry. In addition, to investigate the effect of these interactions in the main metabolic pathways, we have determined the transcriptional response of these interactors to telomerase deficiency by real-time quantitative gene expression analysis. This data will provide us novel insights into telomerase regulation in these parasitic protozoa.
Keywords: RNA-protein interactions , Telomerase , Interactome