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http://purl.uniprot.org/citations/28666385http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28666385http://www.w3.org/2000/01/rdf-schema#comment"Ribosomal proteins are involved in many cellular processes through interactions with various RNAs. Here, applying the photoactivatable-ribonucleoside-enhanced cross-linking and immunoprecipitation approach to HEK293 cells overproducing ribosomal protein (rp) eS1, we determined the products of RNU5A-1 and RNU11 genes encoding U5 and U11 snRNAs as the RNA partners of ribosome-unbound rp eS1. U11 pre-snRNA-associated rp eS1 was revealed in the cytoplasm and nucleus where rp eS1-bound U11/U12 di-snRNP was also found. Utilizing recombinant rp eS1 and 4-thiouridine-containing U11 snRNA transcript, we identified an N-terminal peptide contacting the U-rich sequence in the Sm site-containing RNA region. We also showed that the rp eS1 binding site on U11 snRNA is located in the cleft between stem-loops I and III and that its structure mimics the respective site on the 18S rRNA. It was found that cell depletion of rp eS1 leads to a decrease in the splicing efficiency of minor introns and to an increase in the level of U11 pre-snRNA with the unprocessed 3' terminus. Our findings demonstrate the engagement of human rp eS1 in events related to the U11 snRNA processing and to minor-class splicing. Contacts of rp eS1 with U5 snRNA in the minor pre-catalytic spliceosome are discussed."xsd:string
http://purl.uniprot.org/citations/28666385http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkx559"xsd:string
http://purl.uniprot.org/citations/28666385http://purl.uniprot.org/core/author"Karpova G.G."xsd:string
http://purl.uniprot.org/citations/28666385http://purl.uniprot.org/core/author"Gopanenko A.V."xsd:string
http://purl.uniprot.org/citations/28666385http://purl.uniprot.org/core/author"Kabilov M.R."xsd:string
http://purl.uniprot.org/citations/28666385http://purl.uniprot.org/core/author"Malygin A.A."xsd:string
http://purl.uniprot.org/citations/28666385http://purl.uniprot.org/core/author"Tupikin A.E."xsd:string
http://purl.uniprot.org/citations/28666385http://purl.uniprot.org/core/author"Laktionov P.P."xsd:string
http://purl.uniprot.org/citations/28666385http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28666385http://purl.uniprot.org/core/name"Nucleic Acids Res"xsd:string
http://purl.uniprot.org/citations/28666385http://purl.uniprot.org/core/pages"9121-9137"xsd:string
http://purl.uniprot.org/citations/28666385http://purl.uniprot.org/core/title"Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA."xsd:string
http://purl.uniprot.org/citations/28666385http://purl.uniprot.org/core/volume"45"xsd:string
http://purl.uniprot.org/citations/28666385http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28666385
http://purl.uniprot.org/citations/28666385http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28666385
http://purl.uniprot.org/uniprot/#_B7Z3M5-mappedCitation-28666385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28666385
http://purl.uniprot.org/uniprot/#_A8K4W0-mappedCitation-28666385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28666385
http://purl.uniprot.org/uniprot/#_D6R9B6-mappedCitation-28666385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28666385
http://purl.uniprot.org/uniprot/#_P61247-mappedCitation-28666385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28666385
http://purl.uniprot.org/uniprot/#_Q6NXR8-mappedCitation-28666385http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28666385
http://purl.uniprot.org/uniprot/P61247http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28666385
http://purl.uniprot.org/uniprot/D6R9B6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28666385
http://purl.uniprot.org/uniprot/A8K4W0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28666385
http://purl.uniprot.org/uniprot/Q6NXR8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28666385