HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplementary figures Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Larrondo, L. F. Articles by Vicuña, R. Search for Related Content PubMed PubMed Citation Articles by Larrondo, L. F. Articles by Vicuña, R. Agricola Articles by Larrondo, L. F. Articles by Vicuña, R.

Cloning and characterization of the genes encoding the high-affinity iron-uptake protein complex Fet3/Ftr1 in the basidiomycete Phanerochaete chrysosporium

Luis F. Larrondo^,

Paulo Canessa

Rubén Polanco

Departamento de Genética Molecular y Microbiología, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile and Instituto Milenio de Biología Fundamental y Aplicada, Santiago, Chile

Correspondence
Rafael Vicuña
rvicuna{at}bio.puc.cl

MCO1, a multicopper oxidase from Phanerochaete chrysosporium exhibiting strong ferroxidase activity, has recently been described. This enzyme shows biochemical and structural similarities with the yeast Fet3p, a type I membrane glycoprotein that efficiently oxidizes Fe(II) to Fe(III) for its subsequent transport to the intracellular compartment by the iron permease Ftr1p. The genome database of P. chrysosporium was searched to verify whether it includes a canonical fet3 in addition to mco1, and single copies of fet3 and ftr1 orthologues were found, separated by a divergent promoter. Pc-fet3 encodes a 628 aa protein that exhibits overall identities of about 40 % with other reported Fet3 proteins. In addition to a secretion signal, it has a C-terminal transmembrane domain, characteristic of these cell-surface-attached ferroxidases. Structural modelling of Pc-Fet3 revealed that the active site has all the residues known to be essential for ferroxidase activity. Pc-ftr1 encodes a 393 aa protein that shows about 38 % identity with several Ftr1 proteins from ascomycetes. Northern hybridization studies showed that the mRNA levels of both genes are reduced upon supplementation of the growth medium with iron, supporting the functional coupling of Fet3 and Ftr1 proteins in vivo.

These authors contributed equally to this work.

Present address: Department of Genetics, Dartmouth Medical School, Hanover, NH 03755, USA.

Present address: Depto de Ciencias Biológicas, Facultad de Ciencias de la Salud, Universidad Andrés Bello, Av. República 217, Santiago, Chile.

The GenBank/EMBL/DDBJ accession numbers for the cDNA sequences of Pc-fet3 and Pc-ftr1 are DQ464016 and DQ464017, respectively.

Two supplementary multiple-sequence alignments are available with the online version of this paper.

This article has been cited by other articles:

				V. Gomez-Toribio, A. B. Garcia-Martin, M. J. Martinez, A. T. Martinez, and F. Guillen Induction of Extracellular Hydroxyl Radical Production by White-Rot Fungi through Quinone Redox Cycling Appl. Envir. Microbiol., June 15, 2009; 75(12): 3944 - 3953. [Abstract] [Full Text] [PDF]

				A. Nodop, D. Pietsch, R. Hocker, A. Becker, E. K. Pistorius, K. Forchhammer, and K.-P. Michel Transcript Profiling Reveals New Insights into the Acclimation of the Mesophilic Fresh-Water Cyanobacterium Synechococcus elongatus PCC 7942 to Iron Starvation Plant Physiology, June 1, 2008; 147(2): 747 - 763. [Abstract] [Full Text] [PDF]

				P. Canessa, J. M. Alvarez, R. Polanco, P. Bull, and R. Vicuna The copper-dependent ACE1 transcription factor activates the transcription of the mco1 gene from the basidiomycete Phanerochaete chrysosporium Microbiology, February 1, 2008; 154(2): 491 - 499. [Abstract] [Full Text] [PDF]