期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 24, 期 9, 页码 752-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3439
关键词
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资金
- US National Institutes of Health [R01 GM 106386]
- iNEXT project [2259]
- Forschergruppe FOR [1805]
- Deutsche Forschungsgemeinschaft (DFG) [Sonderforschungsbereich SFB860]
Many antibiotics stop bacterial growth by inhibiting different steps of protein synthesis. However, no specific inhibitors of translation termination are known. Proline-rich antimicrobial peptides, a component of the antibacterial defense system of multicellular organisms, interfere with bacterial growth by inhibiting translation. Here we show that Api137, a derivative of the insect-produced antimicrobial peptide apidaecin, arrests terminating ribosomes using a unique mechanism of action. Api137 binds to the Escherichia coli ribosome and traps release factor (RF) RF1 or RF2 subsequent to the release of the nascent polypeptide chain. A high-resolution cryo-EM structure of the ribosome complexed with RF1 and Api137 reveals the molecular interactions that lead to RF trapping. Api137-mediated depletion of the cellular pool of free release factors causes the majority of ribosomes to stall at stop codons before polypeptide release, thereby resulting in a global shutdown of translation termination.
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