Abstract
The biosynthesis of iron-sulfur (Fe-S) clusters is a highly regulated process involving several proteins. Among them, so-called scaffold proteins play pivotal roles in both the assembly and delivery of Fe-S clusters. Here, we report biochemical properties of HCF101 from Arabidopsis which is involved in biogenesis of [4Fe-4S] proteins including photosystem I (Lezhneva, et al. Plant J. 37, 174-85). We were able to succeed in expressing and purifying HCF101 recombinant protein from E. coli cells. UV/vis absorption spectrum analysis indicated that the purified protein possessed a certain Fe-S cluster-like cofactors, which was sensitive to metal chelation by EDTA or reduction by dithionite. The results of gel filtration analysis of the purified protein and chloroplast stroma fraction suggested that HCF101 existed as a dimer. In addition to the results above, we would like to present the latest data of biochemical studies including an assay of Fe-S cluster transfer from HCF101 to apo-substrate.
