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The Frataxin Homologue Fra Plays a Key Role in Intracellular Iron Channeling in Bacillus subtilis
Author(s) -
Albrecht Alexander G.,
Landmann Hannes,
Nette David,
Burghaus Olaf,
Peuckert Florian,
Seubert Andreas,
Miethke Marcus,
Marahiel Mohamed A.
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100190
Subject(s) - frataxin , bacillus subtilis , aconitase , intracellular , iron binding proteins , biochemistry , mutant , chemistry , iron–sulfur cluster , biosynthesis , biology , bacteria , enzyme , genetics , gene
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 Δ 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 .