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http://purl.uniprot.org/citations/30447990http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30447990http://www.w3.org/2000/01/rdf-schema#comment"Although RNase Y acts as the key enzyme initiating messenger RNA decay in Bacillus subtilis and likely in many other Gram-positive bacteria, its three-dimensional structure remains unknown. An antibody belonging to the rare immunoglobulin G (IgG) 2b λx isotype was raised against a 12-residue conserved peptide from the N-terminal noncatalytic domain of B. subtilis RNase Y (BsRNaseY) that is predicted to be intrinsically disordered. Here, we show that this domain can be produced as a stand-alone protein called Nter-BsRNaseY that undergoes conformational changes between monomeric and dimeric forms. Circular dichroism and size exclusion chromatography coupled with multiangle light scattering or with small angle x-ray scattering indicate that the Nter-BsRNaseY dimer displays an elongated form and a high content of α-helices, in agreement with the existence of a central coiled-coil structure appended with flexible ends, and that the monomeric state of Nter-BsRNaseY is favored upon binding the fragment antigen binding (Fab) of the antibody. The dissociation constants of the IgG/BsRNaseY, IgG/Nter-BsRNaseY, and IgG/peptide complexes indicate that the affinity of the IgG for Nter-BsRNaseY is in the nM range and suggest that the peptide is less accessible in BsRNaseY than in Nter-BsRNaseY. The crystal structure of the Fab in complex with the peptide antigen shows that the peptide adopts an elongated U-shaped conformation in which the unique hydrophobic residue of the peptide, Leu6, is completely buried. The peptide/Fab complex may mimic the interaction of a microdomain of the N-terminal domain of BsRNaseY with one of its cellular partners within the degradosome complex. Altogether, our results suggest that BsRNaseY may become accessible for protein interaction upon dissociation of its N-terminal domain into the monomeric form."xsd:string
http://purl.uniprot.org/citations/30447990http://purl.org/dc/terms/identifier"doi:10.1016/j.bpj.2018.10.016"xsd:string
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/author"Durand D."xsd:string
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/author"Golinelli-Pimpaneau B."xsd:string
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/author"Laalami S."xsd:string
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/author"Bou-Nader C."xsd:string
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/author"Assrir N."xsd:string
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/author"Putzer H."xsd:string
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/author"Velours C."xsd:string
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/author"Hardouin P."xsd:string
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/date"2018"xsd:gYear
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/name"Biophys J"xsd:string
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/pages"2102-2113"xsd:string
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/title"Dissociation of the Dimer of the Intrinsically Disordered Domain of RNase Y upon Antibody Binding."xsd:string
http://purl.uniprot.org/citations/30447990http://purl.uniprot.org/core/volume"115"xsd:string
http://purl.uniprot.org/citations/30447990http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/30447990
http://purl.uniprot.org/citations/30447990http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/30447990
http://purl.uniprot.org/uniprot/#_O31774-mappedCitation-30447990http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30447990
http://purl.uniprot.org/uniprot/O31774http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/30447990