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

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dc.catalogadoraba
dc.contributor.authorLarrondo Castro, Luis Fernando
dc.contributor.authorCanessa, P.
dc.contributor.authorMelo Ledermann, Francisco Javier
dc.contributor.authorPolanco, R.
dc.contributor.authorVicuña, Rafael
dc.date.accessioned2025-02-06T19:31:12Z
dc.date.available2025-02-06T19:31:12Z
dc.date.issued2007
dc.description.abstractMCO1, 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.
dc.format.extent9 páginas
dc.fuente.origenSIPA
dc.identifier.doi10.1099/mic.0.2006/003442-0
dc.identifier.eissn1465-2080
dc.identifier.issn1350-0872
dc.identifier.scopusid2-s2.0-34250704724
dc.identifier.urihttps://doi.org/10.1099/mic.0.2006/003442-0
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/102184
dc.identifier.wosidWOS:000247304900009
dc.information.autorucFacultad de Ciencias Biológicas; Larrondo Castro, Luis Fernando; 0000-0002-8832-7109; 3629
dc.information.autorucFacultad de Ciencias Biológicas; Melo Ledermann, Francisco Javier; 0000-0002-0424-5991; 82342
dc.information.autorucFacultad de Ciencias Biológicas; Vicuña, Rafael; S/I; 99063
dc.issue.numero6
dc.language.isoen
dc.nota.accesocontenido parcial
dc.pagina.final1780
dc.pagina.inicio1772
dc.revistaMicrobiology (Reading, England)
dc.rightsacceso restringido
dc.subjectCDH
dc.subjectCellobiose dehydrogenase
dc.subjectMCO
dc.subjectMulticopper oxidase
dc.subjectTM
dc.subjectTransmembrane
dc.subject.ddc570
dc.subject.deweyBiología
dc.subject.ods06 Clean water and sanitation
dc.subject.odspa06 Agua limpia y saneamiento
dc.titleCloning and characterization of the genes encoding the high-affinity iron-uptake protein complex Fet3/Ftr1 in the basidiomycete Phanerochaete chrysosporium
dc.typeartículo
dc.volumen153
sipa.codpersvinculados3629
sipa.codpersvinculados82342
sipa.codpersvinculados99063
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