AI Article Synopsis
- Nonsense suppressors (NonSups) enable the insertion of amino acids at premature termination codons during protein synthesis, known as readthrough.
- A new, highly purified assay was developed to measure direct readthrough caused specifically by NonSups, revealing that 12 out of 16 tested NonSups induce direct readthrough through at least two mechanisms.
- Preliminary experiments using single molecule fluorescence energy transfer show promise for understanding how NonSups function, potentially improving their clinical effectiveness in treating diseases.
Article Abstract
Nonsense suppressors (NonSups) induce "readthrough", i.e., the selection of near cognate tRNAs at premature termination codons and insertion of the corresponding amino acid into nascent polypeptide. Prior readthrough measurements utilized contexts in which NonSups can promote readthrough directly, by binding to one or more of the components of the protein synthesis machinery, or indirectly, by several other mechanisms. Here we utilize a new, highly purified assay to measure exclusively direct nonsense suppressor-induced readthrough. Of 16 NonSups tested, 12 display direct readthrough, with results suggesting that such NonSups act by at least two different mechanisms. In preliminary work we demonstrate the potential of single molecule fluorescence energy transfer measurements to elucidate mechanisms of NonSup-induced direct readthrough, which will aid efforts to identify NonSups having improved clinical efficacy.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6295867 | PMC |
| http://dx.doi.org/10.1021/acsmedchemlett.8b00472 | DOI Listing |
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