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              <p>In plants, iron-sulfur (Fe-S) proteins are involved in crucial processes such as photosynthetic and respiratory electron transfer reactions and multiple metabolic reactions. The Fe-S proteins are first synthesized as apoproteins and the prosthetic groups are inserted into the polypeptide chain through dedicated assembly machineries. Plants have three Fe-S cluster assembly machineries, namely SUF, ISC and CIA, devoted to the maturation of plastidial, mitochondrial and cytosolic-nuclearFe-S proteins, respectively. While most of the ISC components involved are known, the precise molecular mechanisms underlying the late phase of maturation, in particular the trafficking of Fe-S clusters from the assembly machinery to the apoproteins mediated by transfer proteins, are still insufficiently characterized. By combining molecular and genetic approaches, this work aims at deciphering the role(s) of the mitochondrial glutaredoxin S15 (GRXS15) from Arabidopsis thaliana. The purification of recombinant proteins coupled to Fe-S cluster reconstitution experiments under anaerobic conditions show that AtGRXS15 can incorporate a [2Fe-2S] cluster contrary to what was initially thought and that it can be transferred to the mitochondrial ferredoxin 1 (mFDX1). Looking for partners among the ISC machinery members by binary yeast two hybrid experiments, we have confirmed the interaction with BOLA4 and found an interaction with all three ISCA proteins. Hence, although GRXS15 isoforms were only partially able to complement the corresponding yeast mutant, the fact that the putative partners are conserved among kingdoms might suggest that GRXS15 function is similar to its eukaryotic orthologs. In line with this assumption, the complementation of the Fe-S related defects of the isa1/2 or bol1/3 null mutants of Saccharomyces cerevisiae by the mitochondrial ISCA and BOLA isoforms from Arabidopsis indicate that all these isoforms may act together with GRXS15 in the maturation of mitochondrial Fe-S target proteins.</p>
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