Abstract:
: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 DeltasufD strain failed. Radioactive labeling of N-His-FhuF with [35S]methionine showed that the protein was unstable in the DeltasufD mutant.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Patzer SI,Hantke Kdoi
10.1128/JB.181.10.3307-3309.1999keywords:
subject
Has Abstractpub_date
1999-05-01 00:00:00pages
3307-9issue
10eissn
0021-9193issn
1098-5530journal_volume
181pub_type
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更新日期:1993-06-01 00:00:00