Target intelligence / Profile preview

23S ribosomal RNA of the 50S ribosomal subunit (23S rRNA)

Target
23S rRNA
Molecular classification
Ribosomal RNA, Non-coding RNA, Structural component of ribosome, Other
01

Overview

The **23S ribosomal RNA** is a large non-coding RNA molecule (~2900 nucleotides in *E. coli*) that forms an essential part of the **50S large subunit** of prokaryotic and archaeal ribosomes. It constitutes the core catalytic component known as the **peptidyl transferase center**, which is responsible for catalyzing peptide bond formation during protein synthesis. The structure consists of six secondary domains, providing both structural integrity and functional sites critical for translation. Many clinically important antibiotics—including macrolides, lincosamides, oxazolidinones, and chloramphenicol—target this molecule by binding to its active site(s), thereby inhibiting bacterial protein synthesis. Mutations or chemical modifications within key regions confer antibiotic resistance and may impact cell viability or growth phenotypes. The eukaryotic homolog is called **28S rRNA**.[1][2][3][5]

Other names
23S rRNALarge subunit ribosomal RNA (prokaryotic)Peptidyl transferase center RNA (PTC RNA)
02

Mechanism of action

Inhibition of peptide bond formation by binding to the peptidyl transferase center, blocking protein synthesis[2][6]; Prevention of tRNA binding or translocation within the ribosome[2]

03

Biological functions

Catalysis of peptide bond formation (peptidyl transferase activity)[2][6]Structural scaffold for the large ribosomal subunit[3][5]Binding site for tRNAs and antibiotics[2][3]Essential for protein synthesis/translation[2][5]
04

Disease associations

Infection (as a target for antibacterial drugs)[2][6]Other (mutations can affect cell growth and antibiotic resistance)[2]
05

Safety considerations

Off-target effects on mitochondrial or eukaryotic cytoplasmic ribosomes are possible but rare due to structural differences; main concern is development of bacterial resistance through mutations in 23S rRNA genes or methylation modifications that prevent drug binding[2][6].
06

Interacting drugs

Chloramphenicol[2]

3 more in the full profile.

07

Biomarkers

Mutations in specific domains associated with antibiotic resistance can serve as biomarkers for drug susceptibility testing in clinical microbiology labs[2]

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