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Abstract
cTHY28 is a highly conserved, nuclear protein that was identified in a screen of cellular proteins that mediate apoptosis in avian lymphocytes. To determine the cellular function of cTHY28, a co-immunoprecipitation assay was developed to identify proteins that interact with cTHY28. Mass spectrometric analysis of co-immunoprecipitated material from DT-40 lymphocytes revealed three putative interacting proteins: nucleolin, DNA topoisomerase I and elongation factor-2. From a functional perspective, nucleolin is associated with pre-rRNA processing, DNA topoisomerase I relaxes supercoiled DNA, and elongation factor-2 is involved in protein translation. Since these proteins have a direct, protein-protein interaction with cTHY28, it is hypothesized that cTHY28 may augment their cellular function.