Bacterial 23S ribosomal RNA (domains II and V) (23S rRNA (domains II and V))

The bacterial 50S ribosomal subunit, specifically domains II and V of the 23S ribosomal RNA (rRNA), serves as the functional core for protein synthesis in bacteria (Wilson, 2014). Domain V contains the peptidyl transferase center (PTC), which catalyzes peptide bond formation, while domain II forms part of the nascent peptide exit tunnel (NPET) (Dunkle et al., 2010). This region is the primary binding site for several major classes of antibiotics, including macrolides, lincosamides, oxazolidinones, and pleuromutilins (Arenz & Wilson, 2016). These drugs exert their antimicrobial effects by sterically hindering the elongation of the peptide chain or by interfering with the positioning of tRNA substrates within the PTC (StatPearls). Because of the high conservation of these rRNA domains across bacterial species, they are versatile targets for broad-spectrum and narrow-spectrum antibiotics used to treat respiratory, skin, and systemic infections. However, the structural similarity between bacterial 23S rRNA and human mitochondrial rRNA can lead to off-target effects and toxicity, such as myelosuppression (Long & Vester, 2012). Resistance often arises through point mutations in the rRNA or through the action of methyltransferases that modify specific nucleotides within these domains.

Other names

Peptidyl transferase centerPTC50S ribosomal RNALarge ribosomal subunit RNA23S rRNA

Inhibition of bacterial protein synthesis by binding to the peptidyl transferase center (PTC) or the nascent peptide exit tunnel (NPET) within the 50S subunit, thereby blocking peptide bond formation or the progression of the growing polypeptide chain (Wilson, 2014; StatPearls).