ThrRS Background Information Aminoacyl-tRNA synthetases function to catalyze the aminoacylation of tRNAs by their corresponding amino acids, thus linking amino acids with tRNA-contained nucleotide triplets. ThrRS (threonyl-tRNA synthetase), also known as TARS, is a 723 amino acid member of the class-II aminoacyl-tRNA synthetase family that catalyzes the tRNA(Thr)-threonine aminoacylation reaction. Localized to the cytoplasm, ThrRS contains a zinc-binding catalytic domain, a C terminal tRNA-binding domain and an N terminal editing domain. ThrRS has four mobile regions, three of which have a key residue that changes conformation throughout catalysis, thereby mediating the dynamics of the tRNA-amino acid reaction. The fourth mobile region contains an ordering loop which helps to close the active site once the substrate (threonine) is in place.
ThrRS (C-3)
Click on image to enlarge
ThrRS (C-3): sc-166146. Western blot analysis of ThrRS expression in non-transfected 293T: sc-117752 (A), human ThrRS transfected 293T: sc-113560 (B) and HeLa (C) whole cell lysates.