MRP-S22 Inhibitors

Chemical inhibitors of Small ribosomal subunit protein mS22 (MRP-S22) target various stages of protein synthesis, potentially impacting the role of MRP-S22 in the ribosome. Tetracycline and its derivative Doxycycline inhibit protein synthesis by binding to the 30S ribosomal subunit, a critical component of the protein translation machinery. Their mode of action involves preventing the attachment of aminoacyl-tRNA to the mRNA-ribosome complex, which is essential for the elongation phase of protein synthesis. This process could indirectly affect MRP-S22's function in the small ribosomal subunit by disrupting the normal translational process. Similarly, Puromycin induces premature termination of protein synthesis by mimicking an aminoacyl-tRNA, thus leading to the release of incomplete polypeptide chains. This premature termination could indirectly affect the functional role of MRP-S22 in the ribosome.

In addition, Chloramphenicol and Erythromycin, targeting the 50S ribosomal subunit, prevent peptide bond formation and translocation steps, respectively. While these chemicals primarily affect the large ribosomal subunit, their overall impact on protein synthesis could indirectly influence MRP-S22's function in the small subunit. Cycloheximide, inhibiting eukaryotic protein synthesis by blocking the translocation step, could also indirectly affect MRP-S22. Other chemicals like Streptomycin, Gentamicin, Kanamycin, and Neomycin bind to the 30S ribosomal subunit, causing misreading of mRNA and inhibiting initiation and elongation processes, which could have indirect effects on MRP-S22. Ricin and Anisomycin represent more potent inhibitors; Ricin inactivates ribosomes by depurinating rRNA, and Anisomycin inhibits peptide elongation, both potentially disrupting MRP-S22's role. These chemicals, while not directly targeting MRP-S22, could indirectly impact its function by disrupting the essential processes of the ribosome, the cellular machine for which MRP-S22 is a critical component.