Molecular and General Genetics MGG

, Volume 247, Issue 2, pp 199–205 | Cite as

Functional domains of theEscherichia coli ferric uptake regulator protein (Fur)

  • Igor Stojiljkovic
  • Klaus Hantke
Original Paper

Abstract

The functions of N- and C-terminal domains of the Fur repressor ofEscherichia 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-regulatedlacZ fusion gene. The N-terminal domain, when fused to the C-terminal domain of the repressor C1857, repressed a Fur-regulatedlacZ fusion. However, the Fur-CI857 fusion was unable to complement the growth defect of anE. coli fur mutant on fumarate and succinate. The C-terminal domain of Fur, when fused to the N-terminus of CI857, repressed a λP, -regulatedlacZ fusion, indicating dimerization of the chimeric protein, which is a prerequisite for Cl 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.

Key words

Fur protein DNA-binding Repressor Fur-CI chimeric protein Fur dimerization 

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Copyright information

© Springer-Verlag 1995

Authors and Affiliations

  • Igor Stojiljkovic
    • 1
  • Klaus Hantke
    • 1
  1. 1.Mikrobiologie/MembranphysiologieTübingenGermany

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