Biochemical studies suggested that the antimicrobial peptide apidaecin (Api) inhibits protein synthesis by binding in the nascent peptide exit tunnel and trapping the release factor associated with a terminating ribosome. The mode of Api action in bacterial cells had remained unknown. Here, genome-wide analysis revealed that Api arrests translating ribosomes at stop codons and causes pronounced queuing of the trailing ribosomes. By sequestering the available release factors, Api promotes pervasive stop codon bypass, leading to expression of proteins with C-terminal extensions. Api-mediated translation arrest leads to futile activation of the ribosome rescue systems. Understanding the unique mechanism of Api action in living cells may facilitate development of new medicines and research tools for genome exploration.

中文翻译：

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抗菌肽阿迪霉素对翻译终止的全基因组作用

生化研究表明，抗菌肽芹菜素（Api）通过结合在新生肽出口通道中并捕获与终止核糖体相关的释放因子来抑制蛋白质合成。细菌细胞中Api作用的模式仍然未知。在这里，全基因组分析表明，Api将翻译核糖体停在终止密码子上，并引起尾随核糖体的明显排队。通过隔离可用的释放因子，Api促进了普遍的终止密码子旁路，导致具有C端延伸的蛋白质表达。api介导的翻译停滞导致核糖体拯救系统无效的激活。了解活细胞中Api作用的独特机制可能会促进新药和基因组探索研究工具的开发。