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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-04-02
    Description: Cytosine deamination to uracil occurs frequently in cellular DNA. In vitro, RNA polymerase efficiently inserts adenine opposite to uracil, resulting in G to A base substitutions. In vivo, uracil could potentially alter transcriptional fidelity, resulting in production of mutant proteins. This study demonstrates that in nondividing Escherichia coli cells, a DNA template base replaced with uracil in a stop codon in the firefly luciferase gene results in conversion of inactive to active luciferase. The level of transcriptional base substitution is dependent on the capacity to repair uracil. These results provide evidence for a DNA damage-dependent, transcription-driven pathway for generating mutant proteins in nondividing cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Viswanathan, A -- You, H J -- Doetsch, P W -- CA73041/CA/NCI NIH HHS/ -- CA78622/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1999 Apr 2;284(5411):159-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Program in Genetics and Molecular Biology and Departments of Biochemistry and Radiation Oncology, Emory University School of Medicine, Atlanta, GA 30322, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10102819" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pair Mismatch ; Codon, Terminator ; *DNA Damage ; DNA Repair ; DNA, Bacterial/genetics/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Escherichia coli/*genetics/metabolism ; Genes, Reporter ; Luciferases/genetics/metabolism ; *Mutagenesis ; Novobiocin/pharmacology ; Phenotype ; Protein Biosynthesis ; RNA, Bacterial/genetics ; RNA, Messenger/*genetics ; Templates, Genetic ; *Transcription, Genetic ; Uracil/*metabolism
    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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