Biogenesis of iron-sulfur cluster proteins in plastids

Iron-sulfur (Fe-S) clusters are co-factors of proteins that perform a number of biological roles, including electron transfer, redox and non-redox catalysis, regulation of gene expression, and as sensors within all living organisms, prokaryotes and eukaryotes. These clusters are thought to be among the oldest structures found in biological cells. In chloroplasts, Fe-S clusters play a key role in photosynthetic electron transport as well as nitrogen and sulfur assimilation. The capacity of the Fe atom in Fe-S clusters to take up an electron reversibly provides the required electron carrier capacity in these pathways. Iron and sulfur limitation both affect plant primary production and growth. It has long been known that iron deficiency leads to defects in photosynthesis and bleaching in young leaves, phenomena that are closely linked to a defect in chloroplastic photosystem-I (PSI) accumulation, a major Fe-S containing protein complex in plants. Although the functional importance of Fe-S cluster proteins is evident and isolated chloroplasts have been shown to be able to synthesize their own Fe-S clusters, much is yet to be learned about the biosynthesis of Fe-S proteins in plastids. The recent discovery of a NifS-like protein in plastids has hinted to the existence of an assembly machinery related to bacterial Fe-S assembly systems. This chapter aims to summarize what we presently know about the assembly of Fe-S clusters in plants with an emphasis on green plastids.