Amino Acid Starvation and Colicin D Treatment Induce A-site mRNA Cleavage in Escherichia coli

摘要: Abstract Escherichia coli possesses a unique RNase activity that cleaves stop codons in the ribosomal aminoacyl-tRNA binding site (A-site) during inefficient translation termination. This A-site mRNA cleavage allows recycling of arrested ribosomes by facilitating recruitment tmRNA•SmpB ribosome rescue system. To test whether nuclease also sense codons, we induced pausing at each six arginine using three strategies; rare codon usage, starvation, and inactivation tRNAs with colicin D. In instance, within target resulted tmRNA-mediated SsrA-peptide tagging nascent polypeptide. did not require stringent factor ppGpp, or bacterial toxins such as RelE, which mediates similar activity. However, efficiency was modulated identity two immediately upstream (5′ side) codon. Starvation for histidine tryptophan respectively. Thus, is general response to pausing, capable cleaving variety codons. The induction amino acid starvation suggests this may help regulate protein synthesis nutritional stress.