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Question

Erythromycin is an inhibitor of protein synthesis. It acts by:

The correct answer is

binding to 50S subunit of bacterial ribosome, thus inhibiting translocation.

Erythromycin Action on Protein Synthesis

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 Inhibition by Erythromycin

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.

Analyzing the Options

  • Binding to 30S subunit and inhibiting aminoacyl-tRNA binding: Some antibiotics, like tetracyclines, bind to the 30S subunit and interfere with aminoacyl-tRNA binding, but this is not how Erythromycin works.
  • Binding to 50S subunit and inhibiting translocation: This accurately describes the mechanism of Erythromycin. It binds to the 50S subunit and blocks the translocation step.
  • Inhibiting peptidyl transferase activity of eukaryotic 60S ribosomal subunit: Erythromycin is specific for bacterial ribosomes (70S, composed of 30S and 50S subunits) and does not significantly affect eukaryotic ribosomes (80S, composed of 40S and 60S subunits). Also, while it binds near the peptidyl transferase center, its main effect is inhibition of translocation, not directly inhibiting the peptidyl transferase enzyme itself (which forms peptide bonds).
  • Causes premature chain termination by acting as an analog of aminoacyl-tRNA: This mechanism is characteristic of antibiotics like Puromycin, which mimics aminoacyl-tRNA and gets incorporated into the growing chain, causing premature release. This is not how Erythromycin functions.

Therefore, Erythromycin inhibits bacterial protein synthesis by binding to the 50S subunit of the bacterial ribosome and inhibiting the translocation step.

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Important Questions from Protein synthesis and processing

  1. 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?

  2. 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?

  3. Which one of the following RNAs possesses the peptidyltransferase activity?

  4. Which one of the following statements about GAL gene expression is FALSE?

  5. In Trypanosoma, some of the introns generate Y shaped structure in place of a lariat. Such structure is generated during

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