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Fermentation and alternative oxidase contribute to the action of amino acid biosynthesis-inhibiting herbicides

dc.contributor.authorZulet González, Amaia
dc.contributor.authorGil Monreal, Miriam
dc.contributor.authorZabalza Aznárez, Ana
dc.contributor.authorDongen, Joost T. vanes_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 Publikoaes
dc.date.accessioned2017-04-11T16:40:42Z
dc.date.available2017-04-11T16:40:42Z
dc.date.issued2015
dc.descriptionIncluye 1 fichero de datoses_ES
dc.description.abstractAcetolactate synthase inhibitors (ALS-inhibitors) and glyphosate (GLP) are two classes of herbicide that act by the specific inhibition of an enzyme in the biosynthetic pathway of branched-chain or aromatic amino acids, respectively. The physiological effects that are detected after application of these two classes of herbicides are not fully understood in relation to the primary biochemical target inhibition, although they have been well documented. Interestingly, the two herbicides’ toxicity includes some common physiological effects suggesting that they kill the treated plants by a similar pattern despite targeting different enzymes. The induction of aerobic ethanol fermentation and alternative oxidase (AOX) are two examples of these common effects. The objective of this work was to gain further insight into the role of fermentation and AOX induction in the toxic consequences of ALS-inhibitors and GLP. For this, Arabidopsis T-DNA knockout mutants of alcohol dehydrogenase (ADH) 1 and AOX1a were used. The results found in wild-type indicate that both GLP and ALS-inhibitors reduce ATP production by inducing fermentation and alternative respiration. The main physiological effects in the process of herbicide activity upon treated plants were accumulation of carbohydrates and total free amino acids. The effects of the herbicides on these parameters were less pronounced in mutants compared to wild-type plants. The role of fermentation and AOX regarding pyruvate availability is also discussed.en
dc.description.sponsorshipThis work was financially supported through a grant from the Ministerio Espanol de Ciencia y Tecnología (AGL-2010-18621 and AGL-2013-40567-R). A. Zulet and M. Gil-Monreal received funding from fellowships through the Ministerio de Educación and the Universidad Pública de Navarra, respectively.en
dc.format.mimetypeapplication/pdfen
dc.format.mimetypeapplication/zipen
dc.identifier.doi10.1016/j.jplph.2014.12.004
dc.identifier.issn0176-1617 (Print)
dc.identifier.issn1618-1328 (Electronic)
dc.identifier.urihttps://academica-e.unavarra.es/handle/2454/24092
dc.language.isoengen
dc.publisherElsevieren
dc.relation.ispartofJournal of Plant Physiology 175 (2015) 102–112en
dc.relation.projectIDinfo:eu-repo/grantAgreement/MICINN//AGL2010-18621/ES/en
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO//AGL2013-40567-R/ES/en
dc.relation.publisherversionhttp://doi.org/10.1016/j.jplph.2014.12.004
dc.rights© 2014 Elsevier GmbH. The manuscript version is made available under the CC BY-NC-ND 4.0 license.en
dc.rights.accessRightsAcceso abierto / Sarbide irekiaes
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessen
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectGlyphosateen
dc.subjectAcetolactate synthase inhibitorsen
dc.subjectEthanol fermentationen
dc.subjectArabidopsis thalianaen
dc.subjectPhysiological effectsen
dc.titleFermentation and alternative oxidase contribute to the action of amino acid biosynthesis-inhibiting herbicidesen
dc.typeArtículo / Artikuluaes
dc.typeinfo:eu-repo/semantics/articleen
dc.type.versionVersión aceptada / Onetsi den bertsioaes
dc.type.versioninfo:eu-repo/semantics/acceptedVersionen
dspace.entity.typePublication
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relation.isAuthorOfPublicationb62dd25b-6298-44fe-8690-12267f5b3d70
relation.isAuthorOfPublication0085d805-7945-48bf-994f-85bc2c88d92b
relation.isAuthorOfPublication050bc121-21c9-467d-8bb6-611a789b1011
relation.isAuthorOfPublication.latestForDiscoveryff22d7b9-c559-4cf2-980c-9fcbdeeb4ce4

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