Abstract
The highly regulated rate limiting protein in the de novo synthesis of pyrimidines is the CPSase portion of the multi-enzyme CAD. Both full length CAD and the CPSase segment alone have previously been found to co-immunoprecipitate with the DNA damage checkpoint protein Rad9 in vitro. The interaction increases the enzymatic activity of CPSase in vitro twofold. Live cell studies of the interaction are being performed using fluorescence resonance energy transfer (FRET) imaging in order to visualize the interaction in vivo. YFP-CAD and CFP-Rad9 fusion proteins have been constructed for FRET protein-protein interaction analysis. Changes in localization and interaction are being studied in response to DNA damage as well as cell synchronization in an attempt to determine the dynamics of the interactions under different conditions. Preliminary data suggests that CAD is absent from the nucleus, contrary to a previously published study. Thus, the Rad9-CAD interaction may occur in the cytoplasm. The project is funded by the NIH.
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