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http://purl.uniprot.org/citations/7813017http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7813017http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7813017http://www.w3.org/2000/01/rdf-schema#comment"Rat antizyme gene expression requires programmed, ribosomal frameshifting. A novel autoregulatory mechanism enables modulation of frameshifting according to the cellular concentration of polyamines. Antizyme binds to, and destabilizes, ornithine decarboxylase, a key enzyme in polyamine synthesis. Rapid degradation ensues, thus completing a regulatory circuit. In vitro experiments with a fusion construct using reticulocyte lysates demonstrate polyamine-dependent expression with a frameshift efficiency of 19% at the optimal concentration of spermidine. The frameshift is +1 and occurs at the codon just preceding the terminator of the initiating frame. Both the termination codon of the initiating frame and a pseudoknot downstream in the mRNA have a stimulatory effect. The shift site sequence, UCC-UGA-U, is not similar to other known frameshift sites. The mechanism does not seem to involve re-pairing of peptidyl-tRNA in the new frame but rather reading or occlusion of a fourth base."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(95)90450-6"xsd:string
http://purl.uniprot.org/citations/7813017http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(95)90450-6"xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Atkins J.F."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Atkins J.F."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Gesteland R.F."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Gesteland R.F."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Hayashi S."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Hayashi S."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Murakami Y."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Murakami Y."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Miyazaki Y."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Miyazaki Y."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Matsufuji S."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Matsufuji S."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Matsufuji T."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/author"Matsufuji T."xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/pages"51-60"xsd:string
http://purl.uniprot.org/citations/7813017http://purl.uniprot.org/core/pages"51-60"xsd:string