Domains of phenylalanyl‐tRNA synthetase from Thermus thermophilus required for aminoacylation

Open Access
Publisher Website
Google Scholar
Abstract
The contribution of entire domains or particular amino acid residues of the phenylalanyl‐tRNA synthetase (FRS) from Thermus thermophilus to the interaction with tRNAPhe was studied. Removal of domain 8 of the β subunit resulted in drastic reduction of the dissociation constant of the FRS·tRNAPhe complex. Neither the removal of arginine 2 of the β subunit, which makes the only major contact between domains β1–5 and the tRNA, nor the replacement of the conserved proline 473 by glycine had an influence on the aminoacylation activity of the FRS. Thus, the body comprising domains 1–5 of the β subunit may not be essential for efficient aminoacylation of tRNAPhe by the FRS and rather be involved in other functions.