Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/3567
COMPARTIR / EXPORTAR:
logo share SHARE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE

Invitar a revisión por pares abierta
Campo DC Valor Lengua/Idioma
dc.contributor.authorYun, Dae-Jin-
dc.contributor.authorBressan, Ray A.-
dc.contributor.authorPardo, José M.-
dc.date.accessioned2008-04-14T11:29:00Z-
dc.date.available2008-04-14T11:29:00Z-
dc.date.issued1997-06-
dc.identifier.citationProceeddings of the National Academy of Sciences 94(13): 7082–7087 (1997)en_US
dc.identifier.urihttp://hdl.handle.net/10261/3567-
dc.description6 pages, 7 figures, 24 references. Yun, Dae-Jin et al.---
dc.description.abstractStrains of the yeast Saccharomyces cerevisiae differ in their sensitivities to tobacco osmotin, an antifungal protein of the PR-5 family. However, cells sensitive to tobacco osmotin showed resistance to osmotin-like proteins purified from the plant Atriplex nummularia, indicating a strict specificity between the antifungal protein and its target cell. A member of a gene family encoding stress proteins induced by heat and nitrogen limitation, collectively called Pir proteins, was isolated among the genes that conveyed resistance to tobacco osmotin to a susceptible strain. We show that overexpression of Pir proteins increased resistance to osmotin, whereas simultaneous deletion of all PIR genes in a tolerant strain resulted in sensitivity. Pir proteins have been immunolocalized to the cell wall. The enzymatic digestion of the cell wall of sensitive and resistant cells rendered spheroplasts equally susceptible to the cytotoxic action of tobacco osmotin but not to other osmotin-like proteins, indicating that the cell membrane interacts specifically with osmotin and facilitates its action. Our results demonstrate that fungal cell wall proteins are determinants of resistance to antifungal PR-5 proteins.en_US
dc.description.sponsorshipThis work was supported by grants from Pioneer Hi-Bred International, The Consortium for Plant Biotechnology Inc., and U.S. Department of Agriculture Grant 94-37100-0754.en_US
dc.format.extent550578 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoengen_US
dc.publisherNational Academy of Sciences (U.S.)en_US
dc.rightsclosedAccessen_US
dc.titleStress proteins on the yeast cell surface determine resistance to osmotin, a plant antifungal proteinen_US
dc.typeartículoen_US
dc.description.peerreviewedPeer revieweden_US
dc.identifier.e-issn1091-6490-
dc.contributor.funderDepartment of Agriculture (US)-
dc.contributor.funderPioneer Hi-Bred-
dc.contributor.funderConsortium for Plant Biotechnology Research (US)-
dc.identifier.funderhttp://dx.doi.org/10.13039/100004502es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/100001406es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/100000199es_ES
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.languageiso639-1en-
item.fulltextNo Fulltext-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.openairetypeartículo-
Aparece en las colecciones: (IRNAS) Artículos
Show simple item record

CORE Recommender

Page view(s)

388
checked on 23-abr-2024

Google ScholarTM

Check


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.