The proteome is large and dynamic chiefly due to post-translational modifications (PTMs);however, some PTMs such as arginylation are understudied. Arginylation is the post-translational addition of the amino acid Arg to a eukaryotic protein, and this process is catalyzed by the highly-conserved enzyme arginine transferase (ATE1). Post-translational arginylation is essential for normal eukaryotic development, but much remains unknown regarding the mechanism and the regulation of this process. A recently discovered interaction partner of ATE1 is the ligand of ATE1 (Liat1), but the structure and the function of this protein are both enigmatic. In this work, we cloned, overproduced, and attempted to purify mouse wild-type and truncated Liat1 proteins for structural and biophysical studies. While Liat1 can be heterologously overproduced in large quantities, solubility issues required re-folding attempts. On-column and dialysis-based refolding techniques are described. Additionally, we used protein structural modeling to predict the structure of the region of Liat1 that is not intrinsically disordered. These promising results provide the insight into the structure and the function of the first-known protein partner of ATE1.

Expression and purification of the ligand of ATE1 (Liat1) from <i>Mus musculus</i>

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Expression and purification of the ligand of ATE1 (Liat1) from Mus musculus