Aminoacyl-tRNA

The aa-tRNA, along with particular elongation factors, deliver the amino acid to the ribosome for incorporation into the polypeptide chain that is being produced during translation.

[2] Amino acids that are misacylated with the proper tRNA substrate undergo hydrolysis through the deacylation mechanisms possessed by aa-tRNA synthetases.

[5][6] Research into the stability of aa-tRNAs illustrates that the acyl (or ester) linkage is the most important conferring factor, as opposed to the sequence of the tRNA itself.

Branched and aliphatic amino acids (valine and isoleucine) prove to generate the most stable aminoacyl-tRNAs upon their synthesis, with notably longer half lives than those that possess low hydrolytic stability (for example, proline).

[10] Increased ionic strength resulting from sodium, potassium, and magnesium salts has been shown to destabilize the aa-tRNA acyl bond.

[12] All together, the actual stability of the ester bond influences the susceptibility of the aa-tRNA to hydrolysis within the body at physiological pH and ion concentrations.

It is thermodynamically favorable that the aminoacylation process yield a stable aa-tRNA molecule, thus providing for the acceleration and productivity of polypeptide synthesis.

Tetracyclines are considered broad-spectrum antibiotic agents; these drugs exhibit capabilities of inhibiting the growth of both gram-positive and gram-negative bacteria, as well as other atypical microorganisms.

Furthermore, the TetM protein (P21598) is found to allow aminoacyl-tRNA molecules to bind to the ribosomal acceptor site, despite being concentrated with tetracyclines that would typically inhibit such actions.