Protein cross-linking, peroxidase and b-1,3-endoglucanase involved in resistance of pea against Orobanche crenata

9 páginas, 5 figuras -- PAGS nros. 1461-1469

Detalles Bibliográficos
Autores: Pérez de Luque, Alejandro, González-Verdejo, Clara Isabel, Lozano, María Dolores, Dita, Miguel A., Cubero, José I., González-Melendi, Pablo, Risueño, María Carmen, Rubiales, Diego
Tipo de recurso: artículo
Fecha de publicación:2006
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/65274
Acceso en línea:http://hdl.handle.net/10261/65274
Access Level:acceso abierto
Palabra clave:Confocal microscopy
Cytochemistry
glucanase
In situ hybridization
Orobanche crenata
Parasitic plants
peroxidase
Pisum sativum
protein cross-linking
resistance
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spelling Protein cross-linking, peroxidase and b-1,3-endoglucanase involved in resistance of pea against Orobanche crenataPérez de Luque, AlejandroGonzález-Verdejo, Clara IsabelLozano, María DoloresDita, Miguel A.Cubero, José I.González-Melendi, PabloRisueño, María CarmenRubiales, DiegoConfocal microscopyCytochemistryglucanaseIn situ hybridizationOrobanche crenataParasitic plantsperoxidasePisum sativumprotein cross-linkingresistance9 páginas, 5 figuras -- PAGS nros. 1461-1469Root holoparasitic angiosperms, like Orobanche spp, completely lack chlorophyll and totally depend on their host for their supply of nutrients. O. crenata is a severe constraint to the cultivation of legumes and breeding for resistance remains the most economical, feasible, and environmentally friendly method of control. Due to the lack of resistance in commercial pea cultivars, the use of wild relatives for breeding is necessary, and an understanding of the mechanisms underlying host resistance is needed in order to improve screening for resistance in breeding programmes. Compatible and incompatible interactions between O. crenata and pea have been studied using cytochemical procedures. The parasite was stopped in the host cortex before reaching the central cylinder, and accumulation of H2O2, peroxidases, and callose were detected in neighbouring cells. Protein cross-linking in the host cell walls appears as the mechanism of defence, halting penetration of the parasite. In situ hybridization studies have also shown that a peroxidase and a β-glucanase are differently expressed in cells of the resistant host (Pf651) near the penetration point. The role of these proteins in the resistance to O. crenata is discussedThis research was supported by the projects AGL2005-01781, Food-CT2004-50622, and BOS2002-03550Peer reviewedOxford University Press201320132006info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/65274reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttps://dx.doi.org/10.1093/jxb/erj127info:eu-repo/semantics/openAccessoai:digital.csic.es:10261/652742026-05-22T06:33:51Z
dc.title.none.fl_str_mv Protein cross-linking, peroxidase and b-1,3-endoglucanase involved in resistance of pea against Orobanche crenata
title Protein cross-linking, peroxidase and b-1,3-endoglucanase involved in resistance of pea against Orobanche crenata
spellingShingle Protein cross-linking, peroxidase and b-1,3-endoglucanase involved in resistance of pea against Orobanche crenata
Pérez de Luque, Alejandro
Confocal microscopy
Cytochemistry
glucanase
In situ hybridization
Orobanche crenata
Parasitic plants
peroxidase
Pisum sativum
protein cross-linking
resistance
title_short Protein cross-linking, peroxidase and b-1,3-endoglucanase involved in resistance of pea against Orobanche crenata
title_full Protein cross-linking, peroxidase and b-1,3-endoglucanase involved in resistance of pea against Orobanche crenata
title_fullStr Protein cross-linking, peroxidase and b-1,3-endoglucanase involved in resistance of pea against Orobanche crenata
title_full_unstemmed Protein cross-linking, peroxidase and b-1,3-endoglucanase involved in resistance of pea against Orobanche crenata
title_sort Protein cross-linking, peroxidase and b-1,3-endoglucanase involved in resistance of pea against Orobanche crenata
dc.creator.none.fl_str_mv Pérez de Luque, Alejandro
González-Verdejo, Clara Isabel
Lozano, María Dolores
Dita, Miguel A.
Cubero, José I.
González-Melendi, Pablo
Risueño, María Carmen
Rubiales, Diego
author Pérez de Luque, Alejandro
author_facet Pérez de Luque, Alejandro
González-Verdejo, Clara Isabel
Lozano, María Dolores
Dita, Miguel A.
Cubero, José I.
González-Melendi, Pablo
Risueño, María Carmen
Rubiales, Diego
author_role author
author2 González-Verdejo, Clara Isabel
Lozano, María Dolores
Dita, Miguel A.
Cubero, José I.
González-Melendi, Pablo
Risueño, María Carmen
Rubiales, Diego
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Confocal microscopy
Cytochemistry
glucanase
In situ hybridization
Orobanche crenata
Parasitic plants
peroxidase
Pisum sativum
protein cross-linking
resistance
topic Confocal microscopy
Cytochemistry
glucanase
In situ hybridization
Orobanche crenata
Parasitic plants
peroxidase
Pisum sativum
protein cross-linking
resistance
description 9 páginas, 5 figuras -- PAGS nros. 1461-1469
publishDate 2006
dc.date.none.fl_str_mv 2006
2013
2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/65274
url http://hdl.handle.net/10261/65274
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://dx.doi.org/10.1093/jxb/erj127
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869408781372227584
score 15.811543

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