| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7753812 | Journal of Inorganic Biochemistry | 2018 | 11 Pages |
Abstract
The unstructured N-terminus of the metalloregulatory protein YqjI is rich in metal-binding residues but specifically requires two conserved cysteine residues to coordinate nickel-binding with negative allosteric regulation of the DNA-binding domain, thereby inhibiting the YqjI transcriptional repressor function. Based on its function, yqjI should be renamed Ni-responsive Fe-uptake regulator, nfeR.209
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Matthew Blahut, Stephen Dzul, Suning Wang, Ashoka Kandegedara, Nicholas E. Grossoehme, Timothy Stemmler, F. Wayne Outten,