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http://purl.uniprot.org/citations/28741611http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28741611http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28741611http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.3439"xsd:string
http://purl.uniprot.org/citations/28741611http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.3439"xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Rodnina M.V."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Rodnina M.V."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Beckmann R."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Beckmann R."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Berninghausen O."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Berninghausen O."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Wilson D.N."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Wilson D.N."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Vazquez-Laslop N."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Vazquez-Laslop N."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Mankin A.S."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Mankin A.S."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Klepacki D."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Klepacki D."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Graf M."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Graf M."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Maracci C."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Maracci C."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Karki P."xsd:string
http://purl.uniprot.org/citations/28741611http://purl.uniprot.org/core/author"Karki P."xsd:string