In both E. coli and S. cerevisiae, insertion of Fe-S clusters into an apoprotein requires function of specialized Hsp70. It is generally assumed that mitochondria inherited specialized Hsp70, from their bacterial ancestor. However, our phylogenetic analysis demonstrated that the specialized mitochondrial (mt)Hsp70, Ssq1 is only present in a subset of fungi; most eukaryotes have a single mtHsp70, Ssc1. We propose that in the fungal lineage, the gene encoding multifunctional mtHsp70, was duplicated giving rise to specialized Ssq1. As function of mtHsp70 in Fe-S biogenesis requires interactions with specific co-chaperone Jac1, the question arose; how specialization of Ssq1 affected its interactions with Jac1? Jac1 from S. cerevisiae has high affinity to specialized Ssq1 and low affinity to multifunctional Ssc1, whereas Jac1 from Yarrowia lipolytica, a fungi species which contain only single mtHsp70, display reverse specificity. Changes in amino acid sequence and structure of J-domain were responsible for coevolution of Jac1-Ssq1 partners.

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