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B.A. 2008, Rutgers University
Thesis Advisor: Pranela Rameshwar, Ph.D.
Department of Medicine
Friday, May 10, 2013
2:30 P.M., CC H-1196
Human SLX4 associates with multiple proteins to assemble a modular toolkit for repair of specific types of DNA lesions. SLX4 also interacts with telomeric proteins TRF2 and RAP1. However, the molecular mechanism of these interactions and the telomeric function of SLX4 are largely unknown. Here we have characterized the SLX4-TRF2 interaction. Our data reveal that disruption of the SLX4-TRF2 interaction completely abolishes the telomeric localization of SLX4 and SLX4-associated factors. These results suggest that SLX4, together with TRF2, functions as a double-layer scaffold to simultaneously recruit multiple endonucleases to telomeres for recombination-based telomere maintenance. One important function of this scaffold may be to provide a negative feedback mechanism for telomere length regulation catalyzed by the endonuclease activity of SLX1. These results may also provide a molecular basis for the assembly of a telomeric DNA repair toolkit and suggest a role in normal human cells and a number of pathological conditions that are involved in telomere loss or trimming.