Application of Statistical-Thermal Coupling Analysis to Identify Residue-Residue Interaction Networks that Facilitate Coupled-Domain Dynamics in Aminoacyl-tRNA Synthetases

Abstract

Aminoacyl-tRNA synthetases (ARSs) are multi-domain proteins that catalyze covalent attachment of amino acids to the 3'-end of the cognate tRNA molecules. Long-range domain-domain communications are known to play an important role in the function of ARSs. Earlier studies have demonstrated that the coupling of domain motions is important in mediating long-range inter-domain communication in modular proteins. However, the molecular mechanism of coupled-domain motions and long-range communication in ARSs has remained poorly understood. In the present study, the molecular mechanism underlying the coupled-domain motions in ARSs has been probed.