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  • Genes, Bacterial  (2)
  • American Association for the Advancement of Science (AAAS)  (2)
  • 1
    Publication Date: 1983-08-26
    Description: The complete nucleotide sequence of the diphtheria tox228 gene encoding the nontoxic serologically related protein CRM228 has been determined. A comparison of the predicted amino acid sequence with the available amino acid sequences from the wild-type toxin made it possible to deduce essentially the entire nucleotide sequence of the wild-type tox gene. The signal peptide of pro-diphtheria toxin and the putative tox promoter have been identified, a highly symmetrical nucleotide sequence downstream of the toxin gene has been detected; this region may be the corynebacteriophage beta attachment site (attP). The cloned toxin gene was expressed at a low level in Escherichia coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaczorek, M -- Delpeyroux, F -- Chenciner, N -- Streeck, R E -- Murphy, J R -- Boquet, P -- Tiollais, P -- New York, N.Y. -- Science. 1983 Aug 26;221(4613):855-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6348945" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; Diphtheria Toxin/*genetics ; Escherichia coli/genetics ; Gene Expression Regulation ; Genes ; Genes, Bacterial ; Nucleic Acid Conformation ; Operon
    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
    Publication Date: 1983-04-29
    Description: An 831-base pair segment of the corynebacteriophage beta tox-45 genome encoding fragment A of diphtheria toxin was cloned into plasmid pUC8 in Escherichia coli K12. Strains containing recombinant plasmids expressed the adenosine diphosphate ribosyl transferase activity characteristic of fragment A; this activity could be inhibited by polyvalent antiserum to fragment A as well as by the appropriate monoclonal antibodies to diphtheria toxin. The transferase activity was secreted into the periplasmic space of E. coli. These findings have implications for the future construction of genetically engineered chimeric toxins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leong, D -- Coleman, K D -- Murphy, J R -- New York, N.Y. -- Science. 1983 Apr 29;220(4596):515-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6403984" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal/immunology ; Corynebacterium diphtheriae/genetics ; DNA, Recombinant/metabolism ; Diphtheria Toxin/*genetics ; Escherichia coli/*genetics ; Genes, Bacterial ; Plasmids
    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
    BibTip Others were also interested in ...
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