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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-12-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Varmus, H E -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1337-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2825348" target="_blank"〉PubMed〈/a〉
    Keywords: Avian Sarcoma Viruses/genetics ; Cell Transformation, Neoplastic/genetics ; DNA-Binding Proteins/genetics/physiology ; Fungal Proteins/genetics ; *Gene Expression Regulation ; Oncogene Protein p65(gag-jun) ; *Oncogenes ; *Protein Kinases ; Proto-Oncogene Proteins c-jun ; Retroviridae Proteins/genetics/physiology ; Saccharomyces cerevisiae/genetics ; *Saccharomyces cerevisiae Proteins ; Transcription Factors/genetics/physiology ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1985-12-13
    Description: The pol gene of Rous sarcoma virus is positioned downstream of the gag gene in a different, briefly overlapping reading frame; nevertheless, the primary translation product of pol is a gag-pol fusion protein. Two mechanisms, ribosomal frameshifting and RNA splicing, have been considered to explain this phenomenon. The frameshifting model is supported by synthesis of both gag protein and gag-pol fusion protein in a cell-free mammalian translation system programmed by a single RNA species that was synthesized from cloned viral DNA with a bacteriophage RNA polymerase. Under these conditions, the ratio of the gag protein to the fusion protein (about 20 to 1) is similar to that previously observed in infected cells, the frameshifting is specific for the gag-pol junction, and it is unaffected by large deletions in gag. In addition, synthesis of the fusion protein is ten times less efficient in an Escherichia coli cell-free translation system and cannot be explained by transcriptional errors or in vitro modification of the RNA. Ribosomal frameshifting may affect production of other proteins in higher eukaryotes, including proteins encoded by several retroviruses and transposable elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacks, T -- Varmus, H E -- New York, N.Y. -- Science. 1985 Dec 13;230(4731):1237-42.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2416054" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avian Sarcoma Viruses/*genetics ; Base Sequence ; Cell-Free System ; *Gene Expression Regulation ; Gene Products, gag ; Molecular Weight ; *Protein Biosynthesis ; RNA, Messenger/genetics ; RNA, Viral/genetics ; RNA-Directed DNA Polymerase/*genetics ; Rabbits ; Retroviridae Proteins/genetics ; Ribosomes/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Location Call Number Expected Availability
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