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Journal of Bacteriology, May 1999, p. 3307-3309, Vol. 181, No. 10
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

SufS Is a NifS-Like Protein, and SufD Is Necessary for Stability of the [2Fe-2S] FhuF Protein in Escherichia coli

Silke I. Patzer and Klaus Hantke*

Mikrobiologie II, Universität Tübingen, Tübingen, Germany

Received 7 December 1998/Accepted 15 March 1999

Escherichia coli fhuF mutants, a sufS::MudI mutant, and a sufD::MudI mutant were found to have the same phenotype: the inability to use ferrioxamine B as an iron source in a plate assay. In addition, the sufS and sufD genes were shown to be regulated by the iron-dependent Fur repressor. Sequence analysis revealed that the sufS open reading frame corresponds to orf f406. The protein SufS belongs to the family of NifS-like proteins, which supply sulfur for [Fe-S] centers. The protein FhuF contains a [2Fe-2S] center. A mutation in the upstream sufD gene (orf f423) caused the same phenotype. The T7 expression system and a His tag allow the isolation in good yield of the FhuF protein from a wild-type strain. In contrast, overproduction of the protein in a Delta sufD strain failed. Radioactive labeling of N-His-FhuF with [35S]methionine showed that the protein was unstable in the Delta sufD mutant.

* Corresponding author. Mailing address: Mikrobiologie II, Universität Tübingen, Auf der Morgenstelle 28, D-72076 Tübingen, Germany. Phone: 49-7071-2974645. Fax: 49-7071-294634. E-mail: hantke{at}uni-tuebingen.de.

Journal of Bacteriology, May 1999, p. 3307-3309, Vol. 181, No. 10
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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