Biochemical Studies to Explore the Inter-domain Communication in Escherichia coli Prolyl-tRNA Synthetase

Abstract

Aminoacyl-tRNA synthetases (AARSs) are a family of enzymes that catalyze the covalent attachment of amino acids to their corresponding transfer-RNA (tRNA) strands. These enzymes are involved in an important reaction step required for the proper synthesis of viable proteins. Protein dynamics play a crucial role in the communication between domains within these enzymes. Correlated motion, specifically, between residue pairs has been proven to have a significant role in domain-domain communication. These residues on the predicted pathways are engaged in correlated motion, which promotes communication between the different domains of the enzyme. The purpose of this study was to perform site-directed mutagenesis and kinetic studies to investigate the effects of mutations of selected "on-pathway" residues on catalytic activity of ProRS.