The Aminoacyl-tRNA Synthetases and Their Protein–Protein Interactions

The canonical role of each aminoacyl-tRNA synthetase (ARS) is to correctly aminoacylate its cognate tRNA(s) with its corresponding amino acid; the resultant aminoacyl-tRNAs drive protein translation. However, decades of work, particularly in eukaryotes, have led to the elucidation of a variety of non-translational roles for these ubiquitous enzymes. Many canonical and non-canonical ARS activities rely on protein–protein interactions, and mutations are known that either disrupt these interactions or enable new ones in disease states. Fewer ARS–protein interactions are known in archaea and bacteria; these are mostly focused on connections that occur during translation but also include other interesting, multimeric complexes. This review focuses on physical ARS–protein interactions from all three domains of life. The functional impacts of many of these interactions, when known, are discussed.