Bacterial 23S ribosomal RNA domain V (23S rRNA domain V)

The bacterial 23S ribosomal RNA (rRNA) domain V is a central component of the 50S large ribosomal subunit, serving as the catalytic core of the peptidyl transferase center (PTC) (Nissen et al., Science, 2000). This domain is responsible for facilitating peptide bond formation between the aminoacyl-tRNA in the A-site and the peptidyl-tRNA in the P-site during protein translation (Beringer and Rodnina, Molecular Cell, 2007). Additionally, domain V forms the entrance to the nascent peptide exit tunnel (NPET), which guides the growing polypeptide chain out of the ribosome (Wilson, Nature Reviews Microbiology, 2014). Due to its essential role in bacterial survival, it is a major target for diverse classes of antibiotics, including macrolides, lincosamides, streptogramins, oxazolidinones, and pleuromutilins (Schlünzen et al., Nature, 2001). These drugs exert their antimicrobial effects by binding to specific nucleotides within domain V, thereby obstructing the exit tunnel or inhibiting the catalytic activity of the PTC (Dunkle et al., PNAS, 2010). Resistance to these antibiotics often arises through point mutations in the 23S rRNA or through the action of methyltransferases that modify specific residues, such as A2058, to prevent drug binding (Vester and Douthwaite, Antimicrobial Agents and Chemotherapy, 2001).

Other names

Peptidyl transferase centerPTCDomain V of 23S rRNA23S rRNALarge ribosomal subunit RNA

Inhibition of bacterial protein synthesis by binding to the peptidyl transferase center or the nascent peptide exit tunnel, preventing peptide bond formation or blocking the progression of the growing polypeptide chain.