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  • 标题:Purification and characterization of the diphtheria toxin repressor.
  • 本地全文:下载
  • 作者:M P Schmitt ; E M Twiddy ; R K Holmes
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1992
  • 卷号:89
  • 期号:16
  • 页码:7576-7580
  • DOI:10.1073/pnas.89.16.7576
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:The diphtheria toxin repressor gene (dtxR) encodes a protein (DtxR) that regulates transcription of the diphtheria toxin gene (tox) by an iron-dependent mechanism. Cloned dtxR was expressed in Escherichia coli from the phage T7 gene 10 promoter, and DtxR was purified. Specific binding of DtxR to the tox+ operator was dependent on reduction of DtxR and the presence of ferrous ions. DtxR protected a sequence of approximately 30 nucleotide pairs, partially overlapping the tox promoter and containing a region of dyad symmetry, from digestion by DNase I. DtxR exhibited very little binding to the mutant tox-201 operator region and failed to bind to the promoter/operator region of the ferric uptake regulation (fur) gene of E. coli.
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