Molecular characterization of A cellobiohydrolase gene family in the fungus Pleurotus ostreatus

dc.contributor.authorEizmendi Goikoetxea, María Arantzazu
dc.contributor.authorSannia, Giovanni
dc.contributor.authorRamírez Nasto, Lucía
dc.contributor.authorPisabarro de Lucas, Gerardo
dc.contributor.departmentProducción Agrariaes_ES
dc.contributor.departmentNekazaritza Ekoizpenaeu
dc.date.accessioned2018-02-15T10:32:21Z
dc.date.available2018-02-15T10:32:21Z
dc.date.issued2006
dc.descriptionResumen del poster presentado al VI Meeting on Genetics and Cellular Biology of Basidiomycetes (GCBB-VI), organizado por y celebrado en la Universidad Pública de Navarra el 3-6 de junio de 2005.es_ES
dc.description.abstractCellulose is the most abundant biological polymer on Earth. Its chemical composition consists of D-glucose units linked by β-1,4- glycosidic bonds forming linear polymeric chains with a reducing and a non-reducing end. Cellulose chains may either adhere to each other, via hydrophobic and van der Waals interactions, forming crystalline structures or remain more loosely packaged (amorphous cellulose). Consequently, the physical structure and morphology of native cellulose is complex and not uniform. Biological degradation of cellulose depends on the action of three types of enzymes: endoglucanases (E.C.3.2.1.4), cellobiohydrolases (E.C.3.2.1.91) and β-glucosidases (E.C.3.2.1.21). All them hydrolyse β-1,4-glycosidic bonds but they differ on the substrate specificity. Endoglucanases hydrolyse the amorphous regions of the cellulose fibbers generating new reducing and non-reducing ends, cellobiohydrolases attack the molecule ends yielding cellobiose units, and β-glucosidases hydrolyse cellobiose molecules yielding glucose. Cellobiohydrolases can be classified into two groups: type I (CBHI) and type II (CBHII), each having opposite chain-end specificities. CBHI prefer the reducing ends while CBHII act at non-reducing ends. By the screening of a genomic library from the basidiomycete Pleurotus ostreatus var. florida, we have isolated five cbhI genes, named cbhI1, cbhI2, cbhI3, cbhI4 and cbhI5, proving the occurrence of a multigenic family coding for this enzymatic activity. Using this sequences as probe, it has been possible to know the conditions in which are expressed those genes. This has allowed the synthesis of the each gene cDNA and, by comparison of this sequence with the corresponding genomic sequence, the characterization of their structure. On the other hand, using the RFLP technique and a progeny of 80 monokaryons derived from the dikaryon N001, the five genes have been mapped on the linkage map of P. ostreatus var. florida mapping the cbhI1 to the chromosome IV and the others to the chromosome VI.en
dc.format.extent1 p.
dc.format.mimetypeapplication/pdfen
dc.identifier.isbn84-9769-107-5
dc.identifier.urihttps://academica-e.unavarra.es/handle/2454/27260
dc.language.isoengen
dc.publisherUniversidad Pública de Navarra / Nafarroako Unibertsitate Publikoaes
dc.relation.ispartofAntonio G. Pisabarro and Lucía Ramírez (eds.): VI Meeting on Genetics and Cellular Biology of Basidiomycetes (GCBB-VI). Pamplona: Universidad Pública de Navarra / Nafarroako Unibertsitate Publikoa, 2006.es
dc.rights© Autores; Universidad Pública de Navarra. Esta publicación no puede ser reproducida, almacenada o transmitida total o parcialmente, sea cual fuere el medio y el procedimiento, incluidas las fotocopias, sin permiso previo concedido por escrito por los titulares del copyright.es_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.subjectPleurotus ostreatusen
dc.subjectCellobiohydrolasesen
dc.titleMolecular characterization of A cellobiohydrolase gene family in the fungus Pleurotus ostreatusen
dc.typeinfo:eu-repo/semantics/conferenceObject
dc.type.versioninfo:eu-repo/semantics/publishedVersion
dspace.entity.typePublication
relation.isAuthorOfPublication319163ba-19f1-4d8a-96ff-4b4e9a4b6d5e
relation.isAuthorOfPublication7fedbadd-7e13-485e-99cf-252f1a381373
relation.isAuthorOfPublication54daf1c4-f273-4ade-a90e-7df28e761ca7
relation.isAuthorOfPublication.latestForDiscovery7fedbadd-7e13-485e-99cf-252f1a381373

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