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http://purl.uniprot.org/citations/15236960http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15236960http://www.w3.org/2000/01/rdf-schema#comment"The hydrolytic endoribonuclease RNase E, which is widely distributed in bacteria and plants, plays key roles in mRNA degradation and RNA processing in Escherichia coli. The enzymatic activity of RNase E is contained within the conserved amino-terminal half of the 118 kDa protein, and the carboxy-terminal half organizes the RNA degradosome, a multi-enzyme complex that degrades mRNA co-operatively and processes ribosomal and other RNA. The study described herein demonstrates that the carboxy-terminal domain of RNase E has little structure under native conditions and is unlikely to be extensively folded within the degradosome. However, three isolated segments of 10-40 residues, and a larger fourth segment of 80 residues, are predicted to be regions of increased structural propensity. The larger of these segments appears to be a protein-RNA interaction site while the other segments possibly correspond to sites of self-recognition and interaction with the other degradosome proteins. The carboxy-terminal domain of RNase E may thus act as a flexible tether of the degradosome components. The implications of these and other observations for the organization of the RNA degradosome are discussed."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2004.05.046"xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/author"Ilag L.L."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/author"Luisi B.F."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/author"Robinson C.V."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/author"Symmons M.F."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/author"Carpousis A.J."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/author"Kuhnel K."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/author"Chandran V."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/author"Callaghan A.J."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/author"Poljak L."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/author"Aurikko J.P."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/author"Gunter Grossmann J."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/name"J Mol Biol"xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/pages"965-979"xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/title"Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E."xsd:string
http://purl.uniprot.org/citations/15236960http://purl.uniprot.org/core/volume"340"xsd:string
http://purl.uniprot.org/citations/15236960http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15236960
http://purl.uniprot.org/citations/15236960http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15236960
http://purl.uniprot.org/uniprot/P0A6P9#attribution-9E6C926182D41EDA053F91D4F4BF15F4http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15236960
http://purl.uniprot.org/uniprot/P0A6P9#attribution-B10FF6E43C97EA2FAB7004136378C10Bhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15236960
http://purl.uniprot.org/uniprot/P05055#attribution-9E6C926182D41EDA053F91D4F4BF15F4http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15236960
http://purl.uniprot.org/uniprot/P0A8J8#attribution-58834CB9F51A9861F6B4D220FC172E47http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15236960