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Do FeS clusters rule bacterial iron regulation?

Roland Lill1

  • 1Institut für Zytobiologie, Philipps-Universität Marburg, Marburg, Germany; SYNMIKRO Center for Synthetic Microbiology, Philipps-Universität Marburg, Marburg, Germany.

The Journal of Biological Chemistry
|November 14, 2020
PubMed
Summary

The bacterial ferric uptake regulator (Fur) protein may sense iron using an iron-sulfur cluster, not ferrous iron directly. This finding reveals a new mechanism for cellular iron regulation in bacteria.

Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • The bacterial ferric uptake regulator (Fur) protein is crucial for managing cellular iron levels.
  • Fur's known role involves regulating genes for iron uptake, storage, and utilization.
  • The precise mechanism of iron sensing by Fur has remained unconfirmed *in vivo*.

Purpose of the Study:

  • To investigate the direct iron-binding properties of the Fur protein.
  • To elucidate the physiological mechanism by which Fur senses and responds to cellular iron concentrations.

Main Methods:

  • Purification of Fur protein from *Escherichia coli*.
  • Biochemical analysis to confirm iron binding and characterize the bound cofactor.

Main Results:

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  • The purified Fur protein binds an all-Cys-coordinated [2Fe-2S] cluster.
  • This suggests a novel iron-sensing mechanism for Fur.

Conclusions:

  • The bacterial Fur protein utilizes an iron-sulfur cluster for iron sensing.
  • This finding challenges the long-held assumption of direct ferrous iron binding.
  • Fur may function analogously to other metalloproteins involved in iron regulation across different organisms.