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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.
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