Characterization of the role of Nop17, R2TP complex-member, in the cytosolic Fe-S protein assembly (CIA) system in Saccharomyces cerevisiae

Abstract

The R2TP co-chaperone complex (Rvb1, Rvb2, Tah1 and Pih1/ Nop17) is evolutionarily conserved and mediates the interaction of the Hsp90 chaperone with target proteins and complexes. R2TP-Hsp90 assists maturation of several protein complexes, such as box C/D snoRNPs, U4 and U5 snRNP and RNA polymerase II. Nop17 plays a central role in the complex because it acts on the structural cohesion of R2TP-Hsp90 and the identification of target substrates. The PIH1 domain of Nop17 recognizes and binds the DpSDD motif to Hsp90 target proteins. Thus, proteins interacting with Nop17 are potential targets of R2TP and Hsp90 action. The interaction of Nop17 with Dre2 was verified in our laboratory, but not yet described in the literature. Dre2 is a protein that participates in the biogenesis process of proteins with cytosolic and nuclear Fe-S clusters. The fact that Dre2 presents DSDD motif raises the hypothesis that the phosphorylation of this motif is important for its interaction with Nop17. Since Dre2 participates in the Cytosolic Iron-Sulfur Protein Assembly (CIA), its interaction with Nop17 brings the possibility of R2TP-Hsp90 involvement in this system. In this project it is proposed the functional characterization of the interaction between Nop17 and Dre2. (AU)