| http://purl.uniprot.org/citations/30177741 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/30177741 | http://www.w3.org/2000/01/rdf-schema#comment | "To survive under conditions of stress, such as nutrient deprivation, bacterial 70S ribosomes dimerize to form hibernating 100S particles1. In γ-proteobacteria, such as Escherichia coli, 100S formation requires the ribosome modulation factor (RMF) and the hibernation promoting factor (HPF)2-4. Here we present single-particle cryo-electron microscopy structures of hibernating 70S and 100S particles isolated from stationary-phase E. coli cells at 3.0 Å and 7.9 Å resolution, respectively. The structures reveal the binding sites for HPF and RMF as well as the unexpected presence of deacylated E-site transfer RNA and ribosomal protein bS1. HPF interacts with the anticodon-stem-loop of the E-tRNA and occludes the binding site for the messenger RNA as well as A- and P-site tRNAs. RMF facilitates stabilization of a compact conformation of bS1, which together sequester the anti-Shine-Dalgarno sequence of the 16S ribosomal RNA (rRNA), thereby inhibiting translation initiation. At the dimerization interface, the C-terminus of uS2 probes the mRNA entrance channel of the symmetry-related particle, thus suggesting that dimerization inactivates ribosomes by blocking the binding of mRNA within the channel. The back-to-back E. coli 100S arrangement is distinct from 100S particles observed previously in Gram-positive bacteria5-8, and reveals a unique role for bS1 in translation regulation."xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41564-018-0237-0"xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/author | "Beckmann R."xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/author | "Beckert B."xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/author | "Berninghausen O."xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/author | "Wilson D.N."xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/author | "Plitzko J.M."xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/author | "Ignatova Z."xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/author | "Turk M."xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/author | "Czech A."xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/name | "Nat Microbiol"xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/pages | "1115-1121"xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/title | "Structure of a hibernating 100S ribosome reveals an inactive conformation of the ribosomal protein S1."xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://purl.uniprot.org/core/volume | "3"xsd:string |
| http://purl.uniprot.org/citations/30177741 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/30177741 |
| http://purl.uniprot.org/citations/30177741 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/30177741 |
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