Publication:
Proteolytic pathways induced by herbicides that inhibit amino acid biosynthesis

dc.contributor.authorZulet González, Amaia
dc.contributor.authorGil Monreal, Miriam
dc.contributor.authorVillamor, Joji Gracees_ES
dc.contributor.authorZabalza Aznárez, Ana
dc.contributor.authorHoorn, Renier A.L. van deres_ES
dc.contributor.authorRoyuela Hernando, Mercedes
dc.contributor.departmentCiencias del Medio Naturales_ES
dc.contributor.departmentNatura Ingurunearen Zientziakeu
dc.contributor.funderUniversidad Pública de Navarra / Nafarroako Unibertsitate Publikoa
dc.date.accessioned2017-04-11T21:19:42Z
dc.date.available2017-04-11T21:19:42Z
dc.date.issued2013
dc.description.abstractBackground: The herbicides glyphosate (Gly) and imazamox (Imx) inhibit the biosynthesis of aromatic and branched-chain amino acids, respectively. Although these herbicides inhibit different pathways, they have been reported to show several common physiological effects in their modes of action, such as increasing free amino acid contents and decreasing soluble protein contents. To investigate proteolytic activities upon treatment with Gly and Imx, pea plants grown in hydroponic culture were treated with Imx or Gly, and the proteolytic profile of the roots was evaluated through fluorogenic kinetic assays and activity-based protein profiling. Results: Several common changes in proteolytic activity were detected following Gly and Imx treatment. Both herbicides induced the ubiquitin-26 S proteasome system and papain-like cysteine proteases. In contrast, the activities of vacuolar processing enzymes, cysteine proteases and metacaspase 9 were reduced following treatment with both herbicides.Moreover, the activities of several putative serine protease were similarly increased or decreased following treatment with both herbicides. In contrast, an increase in YVADase activity was observed under Imx treatment versus a decrease under Gly treatment. Conclusion: These results suggest that several proteolytic pathways are responsible for protein degradation upon herbicide treatment, although the specific role of each proteolytic activity remains to be determineden
dc.description.sponsorshipA. Zulet and M. Gil-Monreal received funding from Spanish fellowships through the Ministerio de Educación and the Universidad Pública de Navarra, respectively. This work was financially supported through grants from the Spanish Ministry of Education and Science (AGL-2010-18621) and Max Planck Society and the COST Action CM1004 for funding.en
dc.format.mimetypeapplication/pdfen
dc.identifier.doi10.1371/journal.pone.0073847
dc.identifier.issn1932-6203 (Electronic)
dc.identifier.urihttps://academica-e.unavarra.es/handle/2454/24093
dc.language.isoengen
dc.publisherPublic Library of Scienceen
dc.relation.ispartofPLoS ONE 8(9): e73847en
dc.relation.projectIDinfo:eu-repo/grantAgreement/MICINN//AGL2010-18621/ES/en
dc.relation.publisherversionhttps://dx.doi.org/10.1371/journal.pone.0073847
dc.rights© 2013 Zulet et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en
dc.rights.accessRightsAcceso abierto / Sarbide irekiaes
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectProteolytic pathwaysen
dc.subjectGlyphosateen
dc.subjectImazamoxen
dc.subjectHerbicidesen
dc.subjectAmino acid biosynthesisen
dc.titleProteolytic pathways induced by herbicides that inhibit amino acid biosynthesisen
dc.typeArtículo / Artikuluaes
dc.typeinfo:eu-repo/semantics/articleen
dc.type.versionVersión publicada / Argitaratu den bertsioaes
dc.type.versioninfo:eu-repo/semantics/publishedVersionen
dspace.entity.typePublication
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relation.isAuthorOfPublicationb62dd25b-6298-44fe-8690-12267f5b3d70
relation.isAuthorOfPublication0085d805-7945-48bf-994f-85bc2c88d92b
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relation.isAuthorOfPublication.latestForDiscoveryff22d7b9-c559-4cf2-980c-9fcbdeeb4ce4

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