Erythromycin is an inhibitor of protein synthesis. It acts by:
binding to 50S subunit of bacterial ribosome, thus inhibiting translocation.
Erythromycin is a type of antibiotic that belongs to the macrolide class. These antibiotics are widely used to treat bacterial infections.
Antibiotics like Erythromycin work by targeting essential processes in bacterial cells, such as protein synthesis, which are different from those in human cells. This difference is what makes them effective against bacteria without harming the patient's cells.
Protein synthesis in bacteria occurs on ribosomes, which are complex molecular machines made of ribosomal RNA (rRNA) and proteins. Bacterial ribosomes are composed of two subunits: a smaller 30S subunit and a larger 50S subunit. Together, they form the 70S ribosome.
Erythromycin specifically targets the bacterial 50S ribosomal subunit. It binds to a site on this subunit, near the peptidyl transferase center.
Its primary mode of action is to inhibit the process of translocation. Translocation is a critical step in protein synthesis where the ribosome moves along the messenger RNA (mRNA) molecule by one codon after a new peptide bond is formed. This movement is essential to bring the next codon into the A-site (aminoacyl-tRNA binding site) so that the next aminoacyl-tRNA can bind and the polypeptide chain can be extended.
By binding to the 50S subunit, Erythromycin sterically hinders or prevents this movement. When translocation is blocked, the ribosome cannot move to the next codon. This stops the elongation of the polypeptide chain and thus inhibits bacterial protein synthesis.
Therefore, Erythromycin inhibits bacterial protein synthesis by binding to the 50S subunit of the bacterial ribosome and inhibiting the translocation step.
Many organisms encode only 18 aminoacyl-tRNA synthetases (aaRS). These organisms lack aaRS that use Asn or Gln (as one of the substrates) for direct aminoacylation of the tRNAAsn and tRNAGln, respectively. Which one of the following statements represents the correct option?
Precise recognition of tRNAs by their cognate aminoacyl‐tRNA synthetases is crucial for the fidelity of protein synthesis. In the context of the aminoacylation of tRNAAla with its cognate aminoacyl‐tRNA synthetase (AlaRS) and based on the studies on the molecules of Escherichia coli origin, following statements are made. Which one of the statements is INCORRECT?
Which one of the following RNAs possesses the peptidyltransferase activity?
Which one of the following statements about GAL gene expression is FALSE?
In Trypanosoma, some of the introns generate Y shaped structure in place of a lariat. Such structure is generated during