C12orf65_2810006K23Rik Inhibitors

Chemical inhibitors of C12orf65 can execute their inhibitory effects through various mechanisms that disrupt the protein synthesis machinery, essential for the production and function of C12orf65. Cycloheximide is known to interfere with the translational elongation process by inhibiting the translocation step in eukaryotic ribosomes, thus leading to a reduction in the synthesis of C12orf65. Similarly, anisomycin targets peptidyl transferase activity on the 60S ribosomal subunit, causing an inhibition in peptide bond formation, which can halt the production of functional C12orf65. Puromycin, by mimicking the structure of aminoacyl-tRNA, causes premature chain termination during protein synthesis. This results in truncated, non-functional polypeptides, undermining the function of C12orf65. Chloramphenicol and tetracycline, along with its derivative doxycycline, bind to the bacterial-like ribosomes found in mitochondria where C12orf65 is localized, preventing aminoacyl-tRNA from entering the A site of the ribosome and thereby inhibiting mitochondrial protein synthesis, including that of C12orf65.

In addition to the above-mentioned inhibitors, emetine binds to the 40S subunit and hinders the translocation step on ribosomes, leading to an inhibition of the mitocondrial translation of C12orf65. Ricin and diphtheria toxin exert their inhibitory action by inactivating the 60S ribosomal subunit and elongation factor 2, respectively, both leading to a cessation of protein synthesis and consequently the inhibition of C12orf65 function. Pactamycin and harringtonine interfere with the initiation and elongation steps of protein synthesis by binding to the 30S ribosomal subunit and preventing the addition of new amino acids to the nascent protein chain, affecting the synthesis of C12orf65. Lastly, fusidic acid prevents the release of EF-G from the ribosome, thereby inhibiting the translocation process and consequently the assembly of C12orf65. Each of these inhibitors operates by directly disrupting the ribosomal machinery and the critical processes of translation that are necessary for the production and function of C12orf65, rather than by merely reducing its expression or modulating its activity.