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Characterization of the Role of CG15043 in HeT-A Nuclear Transport

Tara Paravar
Department of Biology,Massachusetts Institute of Technology, Cambridge, MA 02139
Work conducted in Project Lab 7.17

 
   
Non-Scientific Abstract

CResearch shows that an important aspect of aging lies in the function of telomeres, the physical ends of chromosomes.As DNA is replicated during cell division, the chromosomes shorten and important genetic information is lost. Consequently, serious problems can result, such as the development of cancer. To combat this loss, our cells utilize an enzyme, called telomerase, that adds more DNA to the telomeres of our choromosomes. The cells of fruit flies, however, donít have telomerase. Instead, they maintain their telomeres by adding sequences of DNA to the ends of their chromosomes via a mechanism that does not depend on telomerase.This mechanism requires the interaction of proteins both inside and outside of the nucleus. In order to understand these interactions, we have tried to characterize proteins that interact with HeT-A, one of the DNA elements that maintains the fruit fly telomeres. If we can understand different ways that cells are able to preserve their DNA, we might be able to find new treatments to prevent or cure diseases such as cancer and perhaps even to counter the effects of aging.

Abstract

HeT-A is a retrotransposon in Drosophila cells that transposes to the ends of chromosomes and maintains telomeres.The CG15043 protein was one of many proteins shown to interact with HeT-A in a yeast two-hybrid screen. The protein encoded by this gene is novel and is predicted to be a Type I transmembrane protein. To determine whether CG15043 has a role in HeT-A localization, RNAi of CG15043 was added to S2 cells transfected with HeT-A-GFP. In these cells, the localization of HeT-A was not distinctly altered. To understand where CG15043 localizes, the protein was fused to GFP. Results indicate that the CG15043 protein localizes to cytoplasmic organelles or vesicles. The role of this protein in HeT-A localization, however, remains unclear.