title: Iron-sulfur (Fe-S) cluster assembly: the SufBCD complex is a new type of Fe-S scaffold with a flavin redox cofactor.
abstract: Assembly of iron-sulfur (Fe-S) clusters and maturation of Fe-S proteins in vivo require complex machineries. In Escherichia coli, under adverse stress conditions, this process is achieved by the SUF system that contains six proteins as follows: SufA, SufB, SufC, SufD, SufS, and SufE. Here, we provide a detailed characterization of the SufBCD complex whose function was so far unknown. Using biochemical and spectroscopic analyses, we demonstrate the following: (i) the complex as isolated exists mainly in a 1:2:1 (B:C:D) stoichiometry; (ii) the complex can assemble a [4Fe-4S] cluster in vitro and transfer it to target proteins; and (iii) the complex binds one molecule of flavin adenine nucleotide per SufBC(2)D complex, only in its reduced form (FADH(2)), which has the ability to reduce ferric iron. These results suggest that the SufBC(2)D complex functions as a novel type of scaffold protein that assembles an Fe-S cluster through the mobilization of sulfur from the SufSE cysteine desulfurase and the FADH(2)-dependent reductive mobilization of iron.
authors.affiliation: Commissariat à l'Energie Atomique, iRTSV/LCBM, 38054 Grenoble Cedex 09, France.
authors.forename: Silke
authors.initials: S
authors.lastname: Wollers
authors.forename: Gunhild
authors.initials: G
authors.lastname: Layer
authors.forename: Ricardo
authors.initials: R
authors.lastname: Garcia-Serres
authors.forename: Luca
authors.initials: L
authors.lastname: Signor
authors.forename: Martin
authors.initials: M
authors.lastname: Clemancey
authors.forename: Jean-Marc
authors.initials: JM
authors.lastname: Latour
authors.forename: Marc
authors.initials: M
authors.lastname: Fontecave
authors.forename: Sandrine
authors.initials: S
authors.lastname: Ollagnier de Choudens
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D000693:Anaerobiosis; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D005182:Flavin-Adenine Dinucleotide / Q000031:analogs & derivatives* / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D016877:Oxidants / Q000378:metabolism; D010084:Oxidation-Reduction
chemical_list: D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D007506:Iron-Sulfur Proteins; D016877:Oxidants; C498860:SufB protein, E coli; D005182:Flavin-Adenine Dinucleotide; C058805:1,5-dihydro-FAD; D000251:Adenosine Triphosphatases; C507755:SufC protein, E coli
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