PMID:12445820

Citation	Khan, S, Brocklehurst, KR, Jones, GW and Morby, AP (2002) The functional analysis of directed amino-acid alterations in ZntR from Escherichia coli. Biochem. Biophys. Res. Commun. 299:438-45
Abstract	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.
Links	PubMed
Keywords	Amino Acid Sequence; Amino Acids/metabolism; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; 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 Factors/metabolism; Transcription, Genetic
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