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http://purl.uniprot.org/citations/23334891http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23334891http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23334891http://www.w3.org/2000/01/rdf-schema#comment"Arabidopsis COLD SHOCK DOMAIN PROTEIN 3 (AtCSP3) shares an RNA chaperone function with E. coli cold shock proteins and regulates freezing tolerance during cold acclimation. Here, we screened for AtCSP3-interacting proteins using a yeast two-hybrid system and 38 candidate interactors were identified. Sixteen of these were further confirmed in planta interaction between AtCSP3 by a bi-molecular fluorescence complementation assay. We found that AtCSP3 interacts with CONSTANS-LIKE protein 15 and nuclear poly(A)-binding proteins in nuclear speckles. Three 60S ribosomal proteins (RPL26A, RPL40A/UBQ2, and RPL36aB) and the Gar1 RNA-binding protein interacted with AtCSP3 in the nucleolus and nucleoplasm, suggesting that AtCSP3 functions in ribosome biogenesis. Interactions with LOS2/enolase and glycine-rich RNA-binding protein 7 that are cold inducible, and an mRNA decapping protein 5 (DCP5) were observed in the cytoplasm. These data suggest that AtCSP3 participates in multiple complexes that reside in nuclear and cytoplasmic compartments and possibly regulates RNA processing and functioning."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.org/dc/terms/identifier"doi:10.1007/s12192-012-0398-3"xsd:string
http://purl.uniprot.org/citations/23334891http://purl.org/dc/terms/identifier"doi:10.1007/s12192-012-0398-3"xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/author"Sasaki K."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/author"Sasaki K."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/author"Kim M.H."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/author"Kim M.H."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/author"Sonoda Y."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/author"Sonoda Y."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/author"Kaminaka H."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/author"Kaminaka H."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/author"Imai R."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/author"Imai R."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/name"Cell Stress Chaperones"xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/name"Cell Stress Chaperones"xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/pages"517-525"xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/pages"517-525"xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/title"Interactome analysis reveals versatile functions of Arabidopsis COLD SHOCK DOMAIN PROTEIN 3 in RNA processing within the nucleus and cytoplasm."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/title"Interactome analysis reveals versatile functions of Arabidopsis COLD SHOCK DOMAIN PROTEIN 3 in RNA processing within the nucleus and cytoplasm."xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/volume"18"xsd:string
http://purl.uniprot.org/citations/23334891http://purl.uniprot.org/core/volume"18"xsd:string