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dc.creatorFernández Fueyo, Elenaes_ES
dc.creatorRuiz Dueñas, Francisco J.es_ES
dc.creatorFerreira, Patriciaes_ES
dc.creatorFloudas, Dimitrioses_ES
dc.creatorLavín Trueba, José Luises_ES
dc.creatorOguiza Tomé, José Antonioes_ES
dc.creatorPérez Garrido, Gumersindaes_ES
dc.creatorPisabarro de Lucas, Gerardoes_ES
dc.creatorRamírez Nasto, Lucíaes_ES
dc.creatorSantoyo Santos, Franciscoes_ES
dc.date.accessioned2018-12-28T09:14:05Z
dc.date.available2018-12-28T09:14:05Z
dc.date.issued2012
dc.identifier.issn0027-8424 (Print)
dc.identifier.issn1091-6490 (Electronic)
dc.identifier.urihttps://hdl.handle.net/2454/31886
dc.description.abstractEfficient lignin depolymerization is unique to the wood decay basidiomycetes, collectively referred to as white rot fungi. Phanerochaete chrysosporium simultaneously degrades lignin and cellulose, whereas the closely related species, Ceriporiopsis subvermispora, also depolymerizes lignin but may do so with relatively little cellulose degradation. To investigate the basis for selective ligninolysis, we conducted comparative genome analysis of C. subvermispora and P. chrysosporium. Genes encoding manganese peroxidase numbered 13 and five in C. subvermispora and P. chrysosporium, respectively. In addition, the C. subvermispora genome contains at least seven genes predicted to encode laccases, whereas the P. chrysosporium genome contains none. We also observed expansion of the number of C. subvermispora desaturase-encoding genes putatively involved in lipid metabolism. Microarray-based transcriptome analysis showed substantial up-regulation of several desaturase and MnP genes in wood-containing medium. MS identified MnP proteins in C. subvermispora culture filtrates, but none in P. chrysosporium cultures. These results support the importance of MnP and a lignin degradation mechanism whereby cleavage of the dominant nonphenolic structures is mediated by lipid peroxidation products. Two C. subvermispora genes were predicted to encode peroxidases structurally similar to P. chrysosporium lignin peroxidase and, following heterologous expression in Escherichia coli, the enzymes were shown to oxidize high redox potential substrates, but not Mn2+. Apart from oxidative lignin degradation, we also examined cellulolytic and hemicellulolytic systems in both fungi. In summary, the C. subvermispora genetic inventory and expression patterns exhibit increased oxidoreductase potential and diminished cellulolytic capability relative to P. chrysosporium.en
dc.description.sponsorshipThe major portions of this work were performed under US Department of Agriculture Cooperative State, Research, Education, and Extension Service Grant 2007-35504-18257 (to D.C. and R.A.B.). The US Department of Energy Joint Genome Institute is supported by the Office of Science of the US Department of Energy under Contract DE-AC02-05CH11231. This work was supported by Spanish Projects BIO2008-01533 and BIO2011-26694, European Project Peroxidases as Biocatalysts KBBE-2010-4-265397 (to F.J.R.-D. and A.T.M.), the Chilean National Fund for Scientific and Technological Development Grant 1090513 (to L.F.L.), and a “Ramon y Cajal” contract (to F.J.R.-D.).en
dc.format.extent8 p.
dc.format.mimetypeapplication/pdfen
dc.format.mimetypeapplication/zipen
dc.language.isoengen
dc.publisherNational Academy of Sciencesen
dc.relation.ispartofPNAS, April 3, 2012 109 (14) 5458-5463en
dc.subjectCeriporiopsis subvermisporaen
dc.subjectPhanerochaete chrysosporiumen
dc.subjectSelective ligninolysisen
dc.titleComparative genomics of Ceriporiopsis subvermispora and Phanerochaete chrysosporium provide insight into selective ligninolysisen
dc.typeinfo:eu-repo/semantics/articleen
dc.typeArtículo / Artikuluaes
dc.contributor.departmentUniversidad Pública de Navarra. Departamento de Producción Agrariaes_ES
dc.contributor.departmentNafarroako Unibertsitate Publikoa. Nekazaritza Ekoizpena Sailaeu
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessen
dc.rights.accessRightsAcceso abierto / Sarbide irekiaes
dc.identifier.doi10.1073/pnas.1119912109
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/6PN/BIO2011-26694en
dc.relation.publisherversionhttps://doi.org/10.1073/pnas.1119912109
dc.type.versioninfo:eu-repo/semantics/publishedVersionen
dc.type.versionVersión publicada / Argitaratu den bertsioaes


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