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- W2170702959 abstract "Significance Bacteria have a tremendous capacity to rapidly adapt their gene expression profiles and metabolic rates through global regulatory responses. Toxin–antitoxin complexes regulate their own expression under exponential growth but inhibit energy-demanding processes like protein synthesis during stress. A majority of toxins display exquisite endonucleolytic specificity for mRNAs but only in the context of the ribosome. The molecular basis for this selectivity is unclear given their simple microbial RNase architecture. Here, we demonstrate the mechanistic determinants for host inhibition of growth B (HigB) toxin selection of mRNA substrates. Moreover, we propose that ribosome-dependent toxins recognize their mRNA substrates primarily through identification of the third nucleotide of the codon, contrary to how tRNAs and other translation factors also recognize the A site." @default.
- W2170702959 created "2016-06-24" @default.
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- W2170702959 date "2015-10-27" @default.
- W2170702959 modified "2023-10-16" @default.
- W2170702959 title "Defining the mRNA recognition signature of a bacterial toxin protein" @default.
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- W2170702959 doi "https://doi.org/10.1073/pnas.1512959112" @default.
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