Gosset 23S ribosomal RNA of the bacterial 50S ribosomal subunit Overview
23S ribosomal RNA is a large structural and catalytic non-coding RNA comprising about 2,900 nucleotides (in *E. coli*) and is an essential component of the 50S large subunit of the prokaryotic ribosome[3][4][1][8]. It forms the core of the peptidyl transferase center, which is responsible for catalyzing peptide bond formation during protein synthesis, and provides structural scaffolding for ribosomal proteins and functional sites including tRNA binding[2][3]. The 23S rRNA is divided into six major domains (I-VI), each contributing to ribosome architecture and function[4][8]. Domain V, in particular, contains the major antibiotic-binding sites targeted by several classes of clinically important antibacterial agents, such as macrolides and chloramphenicol[3]. Mutations or chemical modifications in specific nucleotides within the 23S rRNA can disrupt ribosome assembly, impair catalysis, or confer antibiotic resistance, making it both an essential biosynthetic enzyme (ribozyme) and a key antibacterial drug target in pathogenic bacteria[3][1][5][6][7].
Mechanism of Action
Inhibition of peptide bond formation (e.g., via binding at the peptidyl transferase center); Inhibition of aminoacyl-tRNA binding or translocation; Allosteric inhibition of ribosome assembly or function
Biological Functions
Disease Associations
Safety Considerations
- Emergence of antibiotic resistance mutations in 23S rRNA leading to therapy failure[3]
- Potential off-target effects if eukaryotic ribosomes are inadvertently affected by drugs (rare)
Interacting Drugs
Associated Biomarkers
| Biomarker |
|---|
| 23S rRNA mutations as markers of antibiotic resistance (e.g., mutations conferring macrolide or chloramphenicol resistance[3]) |
| 23S rRNA methylation status |