Dissection of two distinct defense-related responses to agar oligosaccharides in <i>Gracilaria chilensis</i> (Rhodophyta) and <i>Gracilaria conferta</i> (Rhodophyta)

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dc.contributor.authorWeinberger, F
dc.contributor.authorLeonardi, P
dc.contributor.authorMiravalles, A
dc.contributor.authorCorrea, JA
dc.contributor.authorLion, U
dc.contributor.authorKloareg, B
dc.contributor.authorPotin, P
dc.date.accessioned2025-01-21T01:06:50Z
dc.date.available2025-01-21T01:06:50Z
dc.date.issued2005
dc.description.abstractThe two agar-producing red algae, Gracilaria chilensis C. J. Bird, McLachlan & E. C. Oliveira and Gracilaria conferta (Schousboe ex Montagne) Montagne, responded with hydrogen peroxide (H2O2) release when agar oligosaccharides were added to the medium. In G. conferta, a transient release was observed, followed by a refractory state of 6 h. This response was sensitive to chemical inhibitors of NADPH oxidase, protein kinases, protein phosphatases, and calcium translocation in the cell, whereas it was insensitive to inhibitors of metalloenzymes. Transmission electron microscopic observations of the H2O2-dependent formation of cerium peroxide from cerium chloride indicated oxygen activation at the plasma membrane of G. conferta. A putative system, consisting of a receptor specific to agar oligosaccharides and a plasma membrane-located NADPH oxidase, appears to be responsible for the release of H2O2 in G. conferta. Subcellular examination of G. chilensis showed that the H2O2 release was located in the cell wall. It was sensitive to inhibitors of metalloenzymes and flavoenzymes, and no refractory state was observed. The release was correlated with accumulation of an aldehyde in the algal medium, suggesting that an agar oligosaccharide oxidase is present in the apoplast of G. chilensis. The presence of this enzyme could also be demonstrated by polyacrylamide electrophoresis under nondenaturating conditions and proven to be variable. Cultivation of G. chilensis at 16 to 17 degrees C resulted in significantly stronger expression of agar oligosaccharide oxidase than cultivation at 12 degrees C, which indicates that the enzyme is used under conditions that generally favor microbial agar macerating activity.
dc.fuente.origenWOS
dc.identifier.doi10.1111/j.0022-3646.2005.05009.x
dc.identifier.eissn1529-8817
dc.identifier.issn0022-3646
dc.identifier.urihttps://doi.org/10.1111/j.0022-3646.2005.05009.x
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/96229
dc.identifier.wosidWOS:000231146000018
dc.issue.numero4
dc.language.isoen
dc.pagina.final873
dc.pagina.inicio863
dc.revistaJournal of phycology
dc.rightsacceso restringido
dc.subjectGracilaria
dc.subjectNADPH oxidase
dc.subjectoligoagar
dc.subjectoligosaccharide
dc.subjectoxidase
dc.subject.ods15 Life on Land
dc.subject.ods13 Climate Action
dc.subject.ods14 Life Below Water
dc.subject.odspa15 Vida de ecosistemas terrestres
dc.subject.odspa13 Acción por el clima
dc.subject.odspa14 Vida submarina
dc.titleDissection of two distinct defense-related responses to agar oligosaccharides in <i>Gracilaria chilensis</i> (Rhodophyta) and <i>Gracilaria conferta</i> (Rhodophyta)
dc.typeartículo
dc.volumen41
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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