RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/28092367http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28092367http://www.w3.org/2000/01/rdf-schema#comment"mRNA localization is an essential mechanism of gene regulation and is required for processes such as stem-cell division, embryogenesis and neuronal plasticity. It is not known which features in the cis-acting mRNA localization elements (LEs) are specifically recognized by motor-containing transport complexes. To the best of our knowledge, no high-resolution structure is available for any LE in complex with its cognate protein complex. Using X-ray crystallography and complementary techniques, we carried out a detailed assessment of an LE of the ASH1 mRNA from yeast, its complex with its shuttling RNA-binding protein She2p, and its highly specific, cytoplasmic complex with She3p. Although the RNA alone formed a flexible stem loop, She2p binding induced marked conformational changes. However, only joining by the unstructured She3p resulted in specific RNA recognition. The notable RNA rearrangements and joint action of a globular and an unfolded RNA-binding protein offer unprecedented insights into the step-wise maturation of an mRNA-transport complex."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.3351"xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/author"Sattler M."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/author"Jansen R.P."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/author"Janowski R."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/author"Niessing D."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/author"Schlundt A."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/author"Stehle R."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/author"Paillart J.C."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/author"Heym R.G."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/author"Edelmann F.T."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/author"Jenner A."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/author"Niedner-Boblenz A."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/author"Syed M.I."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/name"Nat Struct Mol Biol"xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/pages"152-161"xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/title"Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex."xsd:string
http://purl.uniprot.org/citations/28092367http://purl.uniprot.org/core/volume"24"xsd:string
http://purl.uniprot.org/citations/28092367http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28092367
http://purl.uniprot.org/citations/28092367http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28092367
http://purl.uniprot.org/uniprot/P38272#attribution-1A3F7F32E0EF88375A6AAC3F87892062http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/28092367
http://purl.uniprot.org/uniprot/P38272#attribution-588743F88871E0509574BEC445C71549http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/28092367
http://purl.uniprot.org/uniprot/P36068#attribution-588743F88871E0509574BEC445C71549http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/28092367