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Published on: June 30, 2022
The yeast multicopper oxidase Fet3p and the iron permease Ftr1p physically interact
M Carmela Bonaccorsi di Patti1, Rossella Miele, M Eugenia Schininà
1Department of Biochemical Sciences A. Rossi Fanelli, University of Rome La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy. mariacarmela.bonaccorsi@uniroma l.it
Abstract:
High affinity iron uptake in yeast is carried out by a multicomponent system formed by the ferroxidase Fet3p and the iron permease Ftr1p. The currently accepted model predicts that Fet3p and Ftr1p are functionally associated, however, a structural interaction between these two proteins has not been proven yet. The methylotrophic yeast Pichia pastoris has been used to perform cross-linking studies aimed to demonstrate the existence of a Fet3p-Ftr1p complex. Cross-linking of membrane suspensions with the membrane-impermeable reagents DTSSP and BS(3) has evidenced the presence of a high molecular weight band with Fet3p oxidase activity. This band has been purified and subjected to N-terminal sequence analysis. Two sequences were found in the cross-linked species, one of which could be assigned to Fet3p and the other to Ftr1p. This is the first experimental demonstration that Fet3p and Ftr1p are physically associated.
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