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Papers In Press, published online ahead of print December 20, 2004
Biology, University of Leicester, Leicester, Leicestershire LE1 7RH
Corresponding Author: sgm5{at}le.ac.uk
The assembly of iron-sulfur (Fe-S) clusters involves several pathways and in prokaryotes the mobilization of sulfur (SUF) system is paramount for Fe-S biogenesis and repair during oxidative stress. The prokaryotic SUF system consist of six proteins: SufC is an ABC/ATPase which forms a complex with SufB and SufD, SufA acts as a scaffold protein and SufE and SufS are involved in sulfur mobilization from cysteine. Despite the importance of Fe-S proteins in higher plant plastids, little is known regarding plastidic Fe-S cluster assembly. We have recently shown that Arabidopsis harbors an evolutionary conserved plastidic SufC protein (AtNAP7) capable of hydrolyzing ATP and interacting with the SufD homolog AtNAP6. Based on this and the prokaryotic SUF system we speculated that a SufB-like protein may exist in plastids. Here we demonstrate that the Arabidopsis plastid-localized SufB homolog AtNAP1 can complement SufB deficiency in E. coli during oxidative stress. Furthermore, we demonstrate that AtNAP1 can interact with AtNAP7 inside living chloroplasts suggesting the presence of a plastidic AtNAP1/AtNAP6/AtNAP7 complex and remarkable evolutionary conservation of the SUF system. However, in contrast to prokaryotic SufB proteins with no associated ATPase activity we show that AtNAP1 is a Fe-stimulated ATPase and that AtNAP1 is capable of forming homodimers. Our results suggest that AtNAP1 represents an atypical plastidic SufB-like protein important for Fe-S cluster assembly and for regulating Fe homeostasis in Arabidopsis.
J. Biol. Chem, 10.1074/jbc.M413082200
Submitted on November 19, 2004
Revised on December 20, 2004
Accepted on December 20, 2004
AtNAP1 represents an atypical SufB protein in arabidopsis plastids
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