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http://purl.uniprot.org/citations/28468753http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28468753http://www.w3.org/2000/01/rdf-schema#comment"Under stress conditions, such as nutrient deprivation, bacteria enter into a hibernation stage, which is characterized by the appearance of 100S ribosomal particles. In Escherichia coli, dimerization of 70S ribosomes into 100S requires the action of the ribosome modulation factor (RMF) and the hibernation-promoting factor (HPF). Most other bacteria lack RMF and instead contain a long form HPF (LHPF), which is necessary and sufficient for 100S formation. While some structural information exists as to how RMF and HPF mediate formation of E. coli 100S (Ec100S), structural insight into 100S formation by LHPF has so far been lacking. Here we present a cryo-EM structure of the Bacillus subtilis hibernating 100S (Bs100S), revealing that the C-terminal domain (CTD) of the LHPF occupies a site on the 30S platform distinct from RMF Moreover, unlike RMF, the BsHPF-CTD is directly involved in forming the dimer interface, thereby illustrating the divergent mechanisms by which 100S formation is mediated in the majority of bacteria that contain LHPF, compared to some γ-proteobacteria, such as E. coli."xsd:string
http://purl.uniprot.org/citations/28468753http://purl.org/dc/terms/identifier"doi:10.15252/embj.201696189"xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/author"Beckmann R."xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/author"Arenz S."xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/author"Beckert B."xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/author"Berninghausen O."xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/author"Wilson D.N."xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/author"Schafer H."xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/author"Bange G."xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/author"Turgay K."xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/author"Steinchen W."xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/author"Abdelshahid M."xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/name"EMBO J"xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/pages"2061-2072"xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/title"Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization."xsd:string
http://purl.uniprot.org/citations/28468753http://purl.uniprot.org/core/volume"36"xsd:string
http://purl.uniprot.org/citations/28468753http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28468753
http://purl.uniprot.org/citations/28468753http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28468753
http://purl.uniprot.org/uniprot/#_P56849-mappedCitation-28468753http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28468753
http://purl.uniprot.org/uniprot/#_P19946-mappedCitation-28468753http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28468753
http://purl.uniprot.org/uniprot/#_P19947-mappedCitation-28468753http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28468753
http://purl.uniprot.org/uniprot/#_P21464-mappedCitation-28468753http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28468753
http://purl.uniprot.org/uniprot/#_P21465-mappedCitation-28468753http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28468753