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Biochem Biophys Res Commun. 2009 Jan 23;378(4):810-5. doi: 10.1016/j.bbrc.2008.11.138. Epub 2008 Dec 11.

Arabidopsis cytosolic Nbp35 homodimer can assemble both [2Fe-2S] and [4Fe-4S] clusters in two distinct domains.

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Institute for Protein Research, Osaka University, Suita, Japan.


Iron-sulfur proteins play physiologically important roles in a variety of metabolic processes in eukaryotes. In plants, iron-sulfur cluster biosynthesis is known to take place both in mitochondria and chloroplasts. However no components that mediate iron-sulfur cluster delivery in the plant cell cytosol have been identified so far. Here we report identification and characterization of a cytosolic Nbp35 homolog named AtNbp35 from Arabidopsis thaliana. AtNbp35-deficient Arabidopsis mutants were seedling lethal. Unlike the previously characterized yeast ScNbp35 which forms a heterotetramer with ScCfd1, AtNbp35 forms a homodimer in the cytosol and can harbor both [4Fe-4S] and [2Fe-2S] clusters on its amino- and carboxyl-terminal domains, respectively. Taken together, our data suggest that Nbp35 plays a pivotal role in iron-sulfur cluster assembly and delivery in the plant cell cytosol as a bifunctional molecular scaffold.

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