PMID:7753029
| Citation |
Stojiljkovic, I and Hantke, K (1995) Functional domains of the Escherichia coli ferric uptake regulator protein (Fur). Mol. Gen. Genet. 247:199-205 |
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| Abstract |
The functions of N- and C-terminal domains of the Fur repressor of Escherichia coli in promoter recognition and dimerization were studied. We investigated the ability of fusion proteins containing the N- or C-terminal domain of Fur to dimerize and to repress a Fur-regulated lacZ fusion gene. The N-terminal domain, when fused to the C-terminal domain of the repressor CI857, repressed a Fur-regulated lacZ fusion. However, the Fur-CI857 fusion was unable to complement the growth defect of an E. coli fur mutant on fumarate and succinate. The C-terminal domain of Fur, when fused to the N-terminus of CI857, repressed a lambda Pr-regulated lacZ fusion, indicating dimerization of the chimeric protein, which is a prerequisite for CI activity. Both fusion proteins were fully active under both iron-rich and iron-poor growth conditions. We conclude that the N-terminal domain of Fur is involved in recognition of the Fur-responsive promoter and the C-terminus mediates oligomerization of the repressor. |
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| Keywords |
Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Base Sequence; DNA Primers; Escherichia coli/genetics; Escherichia coli/metabolism; Molecular Sequence Data; Protein Structure, Tertiary; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Repressor Proteins/genetics; Repressor Proteins/metabolism |
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