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http://purl.uniprot.org/citations/7736590http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7736590http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7736590http://www.w3.org/2000/01/rdf-schema#comment"We have identified an essential gene, called FIP1, encoding a 327 amino acid protein interacting with yeast poly(A) polymerase (PAP1) in the two-hybrid assay. Recombinant FIP1 protein forms a 1:1 complex with PAP1 in vitro. At 37 degrees C, a thermosensitive allele of FIP1 shows a shortening of poly(A) tails and a decrease in the steady-state level of actin transcripts. When assayed for 3'-end processing in vitro, fip1 mutant extracts exhibit normal cleavage activity, but fail to polyadenylate the upstream cleavage product. Polyadenylation activity is restored by adding polyadenylation factor I (PF I). Antibodies directed against FIP1 specifically recognize a polypeptide in these fractions. Coimmunoprecipitation experiments reveal that RNA14, a subunit of cleavage factor I (CF I), directly interacts with FIP1, but not with PAP1. We propose a model in which PF I tethers PAP1 to CF I, thereby conferring specificity to poly(A) polymerase for pre-mRNA substrates."xsd:string
http://purl.uniprot.org/citations/7736590http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(95)90391-7"xsd:string
http://purl.uniprot.org/citations/7736590http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(95)90391-7"xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/author"Keller W."xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/author"Keller W."xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/author"Lingner J."xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/author"Lingner J."xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/author"Minvielle-Sebastia L."xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/author"Minvielle-Sebastia L."xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/author"Preker P.J."xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/author"Preker P.J."xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/pages"379-389"xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/pages"379-389"xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/title"The FIP1 gene encodes a component of a yeast pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase."xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/title"The FIP1 gene encodes a component of a yeast pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase."xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/volume"81"xsd:string
http://purl.uniprot.org/citations/7736590http://purl.uniprot.org/core/volume"81"xsd:string
http://purl.uniprot.org/citations/7736590http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7736590
http://purl.uniprot.org/citations/7736590http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7736590