Probing the Role of Highly Conserved Lysine (K279) Residue in the Editing Domain of Bacterial Prolyl-tRNA Synthetases

Abstract

The Escherichia coli (Ec) prolyl-tRNA synthetase enzyme possesses three distinct domains. One of the domains, the editing domain, is critical for proofreading the charged tRNAPro, ensuring the correct amino acid has been attached to the tRNA molecule. In this editing domain, a highly conserved lysine has been found to be absolutely essential for proofreading. Through site-directed mutagenesis and enzyme kinetic studies this study attempted to probe the role of this lysine residue (K279).