The functional analysis of directed amino-acid alterations in ZntR from Escherichia coli.
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.
Khan
Saira
S
School of Biosciences, Cardiff University, Museum Avenue, Cardiff CF, UK.
Brocklehurst
Kathryn R
KR
Jones
Gareth W
GW
Morby
Andrew P
AP
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D017930:Genes, Reporter; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011401:Promoter Regions, Genetic; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D014157:Transcription Factors / Q000235:genetics* / Q000378:metabolism; D014158:Transcription, Genetic
D000596:Amino Acids; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D014157:Transcription Factors; C492246:ZntR protein, E coli; C118628:ZntR protein, bacteria