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MerR family transcriptional regulator
MerR family DNA-binding protein
Members of this family of DNA-binding domains are predominantly found in the prokaryotic transcriptional regulator MerR. They adopt a structure consisting of a core of three alpha helices, with an architecture that is similar to that of the 'winged helix' fold [1]. [1]. 12958362. Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR. Changela A, Chen K, Xue Y, Holschen J, Outten CE, O'Halloran TV, Mondragon A;. Science. 2003;301:1383-1387. (from Pfam)
MerR family DNA-binding transcriptional regulator
redox-sensitive transcriptional activator SoxR
redox-sensitive transcriptional activator SoxR mediates responses to stress including exposure to heavy metals, drugs or oxygen radicals
SoxR is a MerR-family homodimeric transcription factor with a 2Fe-2S cluster in each monomer. The motif CIGCGCxxxxxC is conserved. Oxidation of the iron-sulfur cluster activates SoxR. The physiological role in E. coli is response to oxidative stress. It is activated by superoxide, singlet oxygen, nitric oxide (NO), and hydrogen peroxide. In E. coli, SoxR increases expression of transcription factor SoxS; different downstream targets may exist in other species.
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