The functional analysis of directed amino-acid alterations in ZntR from Escherichia coli

Saira Khan, Kathryn R Brocklehurst, Gareth W Jones, Andrew P Morby

Research output: Contribution to journalArticle (Academic Journal)peer-review

29 Citations (Scopus)


The ZntR protein from Escherichia coli is a member of the MerR-family of transcriptional regulatory proteins and acts as a hyper-sensitive transcriptional switch primarily in response to Zn(II) and Cd(II). The binding of metal-ions to ZntR initiates a mechanism that remodels the cognate promoter, increasing its affinity for RNA polymerase. We have introduced site-directed mutations into zntR and shown that cysteine and histidine residues are important for transcriptional control and have an effect on metal-ion preference, sensitivity and magnitude of induction. We propose a three-dimensional model of the N-terminal region of ZntR based upon the coordinates of the MerR-family regulator BmrR.

Original languageEnglish
Pages (from-to)438-45
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 6 Dec 2002


  • Amino Acid Sequence
  • Amino Acids/metabolism
  • Bacterial Proteins/genetics
  • Escherichia coli/genetics
  • Escherichia coli Proteins
  • Genes, Reporter
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Promoter Regions, Genetic
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Transcription Factors/genetics
  • Transcription, Genetic


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