{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1360848658047453056.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1021/ac802354j"}},{"identifier":{"@type":"URI","@value":"https://pubs.acs.org/doi/pdf/10.1021/ac802354j"}},{"identifier":{"@type":"PMID","@value":"19219981"}}],"resourceType":"学術雑誌論文(journal article)","dc:title":[{"@value":"RNA and Protein Complexes of <i>trp</i> RNA-Binding Attenuation Protein Characterized by Mass Spectrometry"}],"description":[{"notation":[{"@value":"We have characterized both wild-type and mutant TRAP (trp RNA-binding attenuation protein) from Bacillus stearothermophilus , and their complexes with RNA or its regulator anti-TRAP protein (AT), by electrospray ionization mass spectrometry (ESI-MS). Wild-type TRAP mainly forms homo-11mer rings. The mutant used carries three copies of the TRAP monomer on a single polypeptide chain so that it associates to form a 12mer ring with four polypeptide molecules. Mass spectra showed that both the wild-type TRAP 11mer and the mutant TRAP 12mer can bind a cognate single-stranded RNA molecule with a molar ratio of 1:1. The crystal structure of wild-type TRAP complexed with AT shows a TRAP 12mer ring surrounded by six AT trimers. However, nanoESI-MS of wild-type TRAP mixed with AT shows four species with different binding stoichiometries, and the complex observed by crystallography represents only a minor species in solution; most of the TRAP remains in an 11mer ring form. Mass spectra of mutant TRAP showed only a single species, TRAP 12mer + six copies of AT trimer, which is observed by crystallography. These results suggest that crystallization selects only the most symmetrical TRAP-AT complex from the solution, whereas ESI-MS can take a \"snapshot\" of all the species in solution."}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1420001326216939264","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"10280728"},{"@type":"NRID","@value":"1000010280728"},{"@type":"NRID","@value":"9000413501164"},{"@type":"NRID","@value":"9000399775366"},{"@type":"NRID","@value":"9000006630016"},{"@type":"NRID","@value":"9000410626601"},{"@type":"NRID","@value":"9000242080438"},{"@type":"NRID","@value":"9000001490589"},{"@type":"NRID","@value":"9000363282859"},{"@type":"NRID","@value":"9000253158868"},{"@type":"NRID","@value":"9000240064574"},{"@type":"NRID","@value":"9000413518707"},{"@type":"NRID","@value":"9000238281510"},{"@type":"NRID","@value":"9000017712935"},{"@type":"NRID","@value":"9000399775365"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/read0074225"}],"foaf:name":[{"@value":"Satoko Akashi"}],"jpcoar:affiliationName":[{"@value":"Yokohama City University, Supramolecular Biology, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380848658047453058","@type":"Researcher","foaf:name":[{"@value":"Masahiro Watanabe"}],"jpcoar:affiliationName":[{"@value":"Yokohama City University, Supramolecular Biology, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380848658047453059","@type":"Researcher","foaf:name":[{"@value":"Jonathan G. Heddle"}],"jpcoar:affiliationName":[{"@value":"Yokohama City University, Supramolecular Biology, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380848658047453057","@type":"Researcher","foaf:name":[{"@value":"Satoru Unzai"}],"jpcoar:affiliationName":[{"@value":"Yokohama City University, Supramolecular Biology, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380848658047453060","@type":"Researcher","foaf:name":[{"@value":"Sam-Yong Park"}],"jpcoar:affiliationName":[{"@value":"Yokohama City University, Supramolecular Biology, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380848658047453184","@type":"Researcher","foaf:name":[{"@value":"Jeremy R. H. Tame"}],"jpcoar:affiliationName":[{"@value":"Yokohama City University, Supramolecular Biology, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00032700"},{"@type":"EISSN","@value":"15206882"}],"prism:publicationName":[{"@value":"Analytical Chemistry"}],"dc:publisher":[{"@value":"American Chemical Society (ACS)"}],"prism:publicationDate":"2009-02-16","prism:volume":"81","prism:number":"6","prism:startingPage":"2218","prism:endingPage":"2226"},"reviewed":"false","url":[{"@id":"https://pubs.acs.org/doi/pdf/10.1021/ac802354j"}],"createdAt":"2009-02-16","modifiedAt":"2023-03-07","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Spectrometry,%20Mass,%20Electrospray%20Ionization","dc:title":"Spectrometry, Mass, Electrospray Ionization"},{"@id":"https://cir.nii.ac.jp/all?q=Tryptophan","dc:title":"Tryptophan"},{"@id":"https://cir.nii.ac.jp/all?q=RNA-Binding%20Proteins","dc:title":"RNA-Binding Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Recombinant%20Proteins","dc:title":"Recombinant Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Geobacillus%20stearothermophilus","dc:title":"Geobacillus stearothermophilus"},{"@id":"https://cir.nii.ac.jp/all?q=Bacterial%20Proteins","dc:title":"Bacterial Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Mutation","dc:title":"Mutation"},{"@id":"https://cir.nii.ac.jp/all?q=RNA","dc:title":"RNA"},{"@id":"https://cir.nii.ac.jp/all?q=Transcription%20Factors","dc:title":"Transcription Factors"}],"project":[{"@id":"https://cir.nii.ac.jp/crid/1040282256984150144","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"19036027"},{"@type":"JGN","@value":"JP19036027"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-19036027/"}],"notation":[{"@language":"ja","@value":"ソフトな相互作用からなる、塩濃度に敏感な複合体の溶液構造の解析"}]},{"@id":"https://cir.nii.ac.jp/crid/1040282257005753856","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"20227009"},{"@type":"JGN","@value":"JP20227009"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-20227009/"}],"notation":[{"@language":"ja","@value":"天然変性タンパク質の動的構造と機能制御機構の解明"},{"@language":"en","@value":"Dynamics of intrinsically disordered proteins and their functional roles"}]}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360283694394454144","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Influence of 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