What happens if aminoacyl-tRNA synthetase is inhibited?
If an inhibitor diminishes activity of one of the RS enzymes, the lack of the aminoacyl-tRNAs causes the ribosome to stall when the corresponding mRNA codon enters the decoding site.
What is the purpose of aminoacyl-tRNA synthetase?
Aminoacyl-tRNA synthetases (ARSs) play a vital role in protein synthesis by linking amino acids to their cognate transfer RNAs (tRNAs). This typical function has been well recognized over the past few decades.
What is RNA synthetase inhibitor antibacterial?
An antibacterial ointment used to treat impetigo and secondary skin infections caused by Staphylococcus aureus and Streptococcus pyogenes.
Which antibiotic prevents binding of aminoacyl-tRNA to the A site?
Tetracyclines
Tetracyclines, including doxycycline, prevent the binding of aminoacyl-tRNA by blocking the A (aminoacyl) site of the 30S ribosome.
Which inhibitor works as mimic of amino acyl tRNA?
HF inhibits a mammalian enzyme that fuses proline to its cognate tRNA during protein synthesis, thereby mimicking amino acid limitation.
Which antibiotics are protein synthesis inhibitors?
Antibiotics can inhibit protein synthesis by targeting either the 30S subunit, examples of which include spectinomycin , tetracycline , and the aminoglycosides kanamycin and streptomycin , or to the 50S subunit, examples of which include clindamycin, chloramphenicol , linezolid , and the macrolides erythromycin .
How do protein synthesis inhibitor antibiotics work?
A protein synthesis inhibitor is a substance that stops or slows the growth or proliferation of cells by disrupting the processes that lead directly to the generation of new proteins. It usually refers to substances, such as antimicrobial drugs, that act at the ribosome level.
What is charged tRNA?
Aminoacyl-tRNA (also aa-tRNA or charged tRNA) is tRNA to which its cognate amino acid is chemically bonded (charged). 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.
Which antibiotic inhibits peptidyl transferase?
The 16-member ring macrolide antibiotics carbomycin, spiramycin, and tylosin inhibit peptidyl transferase.