Identification and characterization of Arginyl-tRNA synthetase translation-independent functions
Biochemistry
Final Report Abstract
Aminoacyl tRNA Synthetases are an ancient protein class that acquired additional domains and functions during the course of evolution. Many of those have been identified only in recent years and play crucial roles in cellular and systemic signal transduction. In this study, we aimed to explore previously unknown functions of arginyl-tRNA Synthetase (ArgRS) in mammalian cells. We found a number of potentially biologically relevant new interaction partners of ArgRS and focused on the verification and characterization of one of them, Serin/arginine-repeat matrix protein 2 (SRRM2), a component of the spliceosome. We could show that under arginine fluctuation, nuclear translocation of ArgRS is increased and am currently studying the implications for alternative protein splicing. This is a highly exciting finding, linking for the first time metabolism sensing and alternative protein splicing regulation by an aaRS in higher eukaryotes. We aim to further study this interaction, its upstream and downstream modulators, and its implication in the context of cancer progression.
