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23S ribosomal RNA (23S rRNA) is a large (2,904 nucleotides in E. coli) non-coding RNA that forms the core structural and functional framework of the 50S large ribosomal subunit in bacteria and archaea. It consists of six structural domains and plays the central catalytic role in the peptidyl transferase center (PTC), facilitating the formation of peptide bonds during protein synthesis[3][6]. The 23S rRNA also provides essential tRNA binding sites and serves as the main binding target for several classes of antibiotics, which act by inhibiting bacterial translation. Mutations in domains of this rRNA are linked to drug resistance and can affect cell growth and ribosome assembly[3][1][4][6]. The bacterial 23S rRNA is phylogenetically distinct and highly conserved among prokaryotes, with its eukaryotic counterpart being the 28S rRNA[3]. Note: The 23S rRNA itself is not a protein, receptor, or enzyme but a fundamental ribonucleic acid molecule with direct catalytic activity and binding properties for both functional (protein synthesis) and therapeutic (antibiotic interaction) applications[3][2][1].
Antibiotics bind to 23S rRNA (often domain V in the peptidyl transferase center), inhibiting peptide bond formation and blocking protein synthesis. This leads to bacterial cell death or stasis
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