MRP-S31 Inhibitors

Emetine, an alkaloid derived from the ipecac root, is known to inhibit protein synthesis by intercalating into DNA and inhibiting DNA topoisomerase II. As MRP-S31 is involved in the mitochondrial ribosomal process, emetine's inhibition of protein synthesis machinery can lead to decreased efficiency of the mitochondrial ribosomes, thus functionally inhibiting MRP-S31 by impairing its role in mitochondrial protein translation.

Chloramphenicol acts by binding to the bacterial 50S ribosomal subunit and inhibiting peptidyl transferase activity. Although MRP-S31 is a mitochondrial ribosome component, chloramphenicol can similarly inhibit mitochondrial protein synthesis by affecting mitochondrial ribosome function, thereby functionally inhibiting MRP-S31 by preventing its participation in protein translation within the mitochondria.

Tetracycline inhibits protein synthesis by binding to the 30S ribosomal subunit and blocking the attachment of aminoacyl-tRNA to the ribosomal acceptor site. This mechanism of action can extend to the mitochondrial ribosome, where it would functionally inhibit MRP-S31 by impeding its contribution to mitochondrial protein translation.

Puromycin is an aminonucleoside antibiotic that causes premature chain termination during protein synthesis by acting as an analog of aminoacyl-tRNA. This leads to the release of nascent polypeptide chains. When puromycin affects mitochondrial protein synthesis, it can functionally inhibit MRP-S31 by disrupting its role in the elongation phase of translation within mitochondria.

Doxycycline, a tetracycline antibiotic, inhibits protein synthesis by binding to the 30S ribosomal subunit and preventing the binding of aminoacyl-tRNA molecules to the ribosome. This action can impair mitochondrial ribosomal function and thereby functionally inhibit MRP-S31 by blocking its involvement in mitochondrial protein synthesis.

Anisomycin interferes with protein synthesis by inhibiting peptidyl transferase activity on the 60S ribosomal subunit. Its action can extend to mitochondrial ribosomes, where it can functionally inhibit MRP-S31 by disrupting peptidyl transferase activity required for mitochondrial protein synthesis.

Cycloheximide blocks the translocation step in protein synthesis by binding to the eukaryotic 80S ribosome. While it predominantly affects cytoplasmic ribosomes, it is also known to affect mitochondrial protein synthesis. By inhibiting the translocation step in mitochondria, cycloheximide can functionally inhibit MRP-S31 by preventing its role in the translation process of mitochondrial proteins.

Dactinomycin binds to DNA and interferes with the DNA-dependent RNA synthesis by inhibiting RNA polymerase. Although it primarily targets nuclear DNA transcription, it can also bind mitochondrial DNA and inhibit transcription there, which indirectly leads to a functional inhibition of MRP-S31 by decreasing the availability of mitochondrial RNA for translation, on which MRP-S31 acts.

Thiostrepton inhibits protein synthesis by binding to the 50S ribosomal subunit and interfering with ribosome function. This mechanism may extend to the mitochondrial ribosome due to structural similarities, thereby potentially inhibiting MRP-S31 by affecting its role in mitochondrial protein synthesis.