Large ribosomal subunit protein uL23 (uL23)

Large ribosomal subunit protein uL23 (commonly called L23 in bacteria) is an essential and highly conserved structural protein component of the bacterial 50S ribosomal subunit[5][8]. It participates early in ribosome assembly, binding 23S rRNA, and is crucial for bacterial cell growth[8]. L23 forms part of the polypeptide exit tunnel, where newly synthesized proteins exit the ribosome, and serves as an interaction platform for protein biogenesis factors, such as the chaperone trigger factor and the signal recognition particle[1][2][8]. It is a critical structural and functional element of the translation machinery, making it a target for some antibiotics that bind near or at the tunnel exit to inhibit protein synthesis[1][2]. The protein's functional equivalents in other organisms include L25 in yeast and L23a in eukaryotes[1][5].

Other names

Ribosomal protein L2350S ribosomal protein L23rplW (gene)ribosomal protein L25 in yeastribosomal protein L23a in some eukaryotes

Inhibition of protein synthesis by binding near the ribosomal exit tunnel, preventing elongation or proper folding of nascent polypeptides