izvor podataka: poirot

Investigation of substrate and editing specificity in tRNA synthetases and the mechanism of antibiotic action

Investigation of substrate and editing specificity in tRNA synthetases and the mechanism of antibiotic action


Proteins are the working horses of the living cell. They are built from twenty amino acids that are attached to one another in a specific order. Aminoacyl-tRNA synthetases (aaRSs) are enzymes that dictate amino acid incorporation into proteins following the information encoded in genes. There are 20 aaRSs in the cell each specific for one amino acid. These enzymes face the difficult task of selecting the designated amino acid from a pool of similar amino acids. Protein functionality strongly depends on the accuracy of amino acid incorporation, making the fidelity of protein synthesis crucial for cell viability. This project aims to delineate the evolutionary and mechanistic basis of aaRSs fidelity. AaRS enzymes are very accurate enzymes that double check that the correct amino acid is chosen. First in the active site of the enzyme and then through additional enzymatic proofreading. We will investigate which characteristics of aaRSs allows them to be fast and at the same time accurate, and to which degree their enzymatic properties may have evolved to prevent binding of substrate-mimicking antibiotics into the active sites. Understanding the molecular mechanisms by which cells ensure high fidelity of protein synthesis under different physiological pressures is of importance for development of new antibiotics and disease treatments.


biosinteza proteina, antibiotska reszistencija, aminoacil-tRNA-sintetaze, točnost translacije

protein biosynthesis, antibiotic resistance, aminoacyl-tRNA syntehtases

Znanstveno-istraživački projekti

nije evidentirano

IZHRZO 180567

01.03.2019

28.02.2022

nije evidentirano

EUR 369.652,00