Mycobacterial ribosomal protein S1 (RpsA)

Mycobacterial ribosomal protein S1 (RpsA, bS1) is a large, highly acidic, and flexible protein (~61 kDa) found on the small subunit (30S) of the mycobacterial ribosome[1][3][4][5]. Composed of four (in mycobacteria) or up to six (in E. coli/Gram-negatives) oligonucleotide/oligosaccharide-binding (OB)-fold domains, it binds single-stranded RNA and is essential for translation initiation on canonical mRNAs by recruiting and stabilizing binding of the mRNA to the ribosome[1][2][3]. In Mycobacterium smegmatis and Mycobacterium tuberculosis, S1 also interacts with unique rRNA segments to protect and stabilize the ribosome during hibernation, which may help bacterial survival during latency or stress[3]. Ribosomal protein S1 is considered a potential, though currently unexploited, antimicrobial target, owing to its crucial role in protein synthesis and ribosome function in mycobacteria[4]. Past hypotheses about it being the direct target of pyrazinamide have been refuted in recent studies[5].

Other names

Ribosomal protein S1bS1RpsA

Not applicable: no clinically validated drugs act directly on Mycobacterial ribosomal protein S1. Previously proposed: inhibition of trans-translation by blocking tmRNA binding (no longer supported for clinical drugs).