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

被引：14

作者：

di Patti, MCB ^{[1
]}

Miele, R ^{[1
]}

Schininà, ME ^{[1
]}

Barra, D ^{[1
]}

机构：

[1] Univ Roma La Sapienza, Dept Biochem Sci A Rossi Fanelli, I-00185 Rome, Italy

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2005年 / 333卷 / 02期

关键词：

Fet3p; Ftr1p; ferroxidase; iron uptake; Pichia pastoris; cross-linking;

D O I：

10.1016/j.bbrc.2005.05.121

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 BS3 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. (c) 2005 Elsevier Inc. All rights reserved.

引用

页码：432 / 437

页数：6

共 21 条

[1]

Askwith C, 1997, J BIOL CHEM, V272, P401

[2] Site-directed mutagenesis of the yeast multicopper oxidase Fet3p [J].

Askwith, CC ;

Kaplan, J .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (35) :22415-22419

[3]

Ausubel FM, 1995, CURRENT PROTOCOLS MO

[4]

Cereghino JL, 2000, FEMS MICROBIOL REV, V24, P45, DOI 10.1016/S0168-6445(99)00029-7

[5] The essential role of Glu-185 and Tyr-354 residues in the ferroxidase activity of Saccharomyces cerevisiae Fet3 [J].

di Patti, MCB ;

Felice, MR ;

Camuti, AP ;

Lania, A ;

Musci, G .

FEBS LETTERS, 2000, 472 (2-3) :283-286

[6] Release of highly active Fet3 from membranes of the yeast Pichia pastoris by limited proteolysis [J].

di Patti, MCB ;

Bellenchi, GC ;

Bielli, P ;

Calabrese, L .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1999, 372 (02) :295-299

[7] A multicopper oxidase gene from Candida albicans:: cloning, characterization and disruption [J].

Eck, R ;

Hundt, S ;

Härtl, A ;

Roemer, E ;

Künkel, W .

MICROBIOLOGY-UK, 1999, 145 :2415-2422

[8] RAPID PRODUCTION OF FULL-LENGTH CDNAS FROM RARE TRANSCRIPTS - AMPLIFICATION USING A SINGLE GENE-SPECIFIC OLIGONUCLEOTIDE PRIMER [J].

FROHMAN, MA ;

DUSH, MK ;

MARTIN, GR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1988, 85 (23) :8998-9002

[9] Molecular mechanisms of iron uptake in fungi [J].

Kosman, DJ .

MOLECULAR MICROBIOLOGY, 2003, 47 (05) :1185-1197

[10] Cloning of Pichia pastoris Fet3:: Insights into the high affinity iron uptake system [J].

Paronetto, MP ;

Miele, R ;

Maugliani, A ;

Borro, M ;

di Patti, MCB .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2001, 392 (01) :162-167

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