期刊
CHEMBIOCHEM
卷 12, 期 13, 页码 2052-2061出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201100190
关键词
Bacillus subtilis; frataxin; iron; metalloproteins; metalloproteomics
资金
- DFG [MA811/23-1]
- Excellence Initiative LOEWE of the state Hessen
Frataxin homologues are important iron chaperones in eukarya and prokarya. Using a native proteomics approach we were able to identify the structural frataxin homologue Fra (formerly YdhG) of Bacillus subtilis and to quantify its native iron-binding stoichiometry. Using recombinant proteins we could show in vitro that Fra is able to transfer iron onto the B. subtilis SUF system for iron-sulfur cluster biosynthesis. In a four-constituents reconstitution system (including SufU, SufS, Fra and CitB) we observed a Fra-dependent formation of a [4 Fe-4 S] cluster on SufU that could be efficiently transferred onto the target apo-aconitase (CitB). A Delta fra deletion mutant showed a severe growth phenotype associated with a broadly disturbed iron homeostasis; this indicates that Fra is a central component of intracellular iron channeling in B. subtilis.
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