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.
Original language | English |
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Pages (from-to) | 438-45 |
Number of pages | 8 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 299 |
Issue number | 3 |
Publication status | Published - 6 Dec 2002 |
Keywords
- 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