The yeast multicopper oxidase Fet3p and the iron permease Ftr1p physically interact.

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.

authors

Bonaccorsi di Patti MC,Miele R,Eugenia Schininà M,Barra D

doi

10.1016/j.bbrc.2005.05.121

subject

Has Abstract

pub_date

2005-07-29 00:00:00

pages

432-7

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(05)01117-4

journal_volume

333

pub_type

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