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Ataluren binds to multiple protein synthesis apparatus sites and competitively inhibits release factor-dependent termination - Nature Communications
Abstract Genetic diseases are often caused by nonsense mutations, but only one TRID (translation readthrough inducing drug), ataluren, has been approved for clinical use. Ataluren inhibits release factor complex (RFC) termination activity, while not affecting productive binding of near-cognate ternary complex (TC, aa-tRNA.eEF1A.GTP).
Probing the interaction between NatA and the ribosome for co-translational protein acetylation
Previous studies showed that the NatA-ribosome interaction is salt dependent in vivo. We performed the same analysis with purified NatA and ribosome. We found that the same held true in our experiment. As the salt concentration increased, the interaction weakened until NatA pull down by the ribosome was undetectable ( Fig 2C ). (A) Representative Western blot of NatA/ribosome co-sedimentation assay with increasing concentration of ribosome. P stands for pellet, and S stands for supernatant.
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