О проекте

Aminoacyl-tRNA synthetases from plants, must come to terms not only with discriminating between the 20 common amino acids but must also contend with related potentially toxic analogues. L-canavanine has been found to occur as a toxic nonprotein amino acid in more than 1500 leguminous plants. One mechanism of its toxicity is its incorporation into proteins, replacing arginine and giving rise to functionally aberrant polypeptides. We have focused our attention on a pair of species specific plant arginyl-tRNA synthetases variants, one of which is said to be evolutionarily adapted to ignore a toxic arginine analogue, while the other lacks this ability. We elucidate that mechanism to determine the features of tRNA that are responsible for triggering the protein conformational change that culminates in the creation of an enzymatic active site that is productive in discriminating between arginine and canavanine.