Publication:
Branched-chain amino acid biosynthesis inhibitors: herbicide efficacy is associated with an induced carbon–nitrogen imbalance

dc.contributor.authorZabalza Aznárez, Ana
dc.contributor.authorZulet González, Amaia
dc.contributor.authorIgal Díaz de Cerio, María
dc.contributor.authorGil Monreal, Miriam
dc.contributor.authorRoyuela Hernando, Mercedes
dc.contributor.departmentCiencias del Medio Naturales_ES
dc.contributor.departmentNatura Ingurunearen Zientziakeu
dc.date.accessioned2017-04-11T21:25:11Z
dc.date.available2017-04-11T21:25:11Z
dc.date.issued2013
dc.description.abstractAcetolactate synthase (ALS; EC 4.1.3.18) and ketol-acid reductoisomerase (KARI; EC 1.1.1.86) are two consecutive enzymes in the biosynthesis of branched-chain amino acids. Several commercial herbicides inhibit ALS as their primary site of action. KARI has also attracted attention as a potential target for herbicides. Although potent and selective inhibitors of KARI have been discovered, these inhibitors display less herbicidal activity than ALS-inhibiting herbicides. To obtain a better understanding of these findings, we have compared the physiological effects induced in pea plants after KARI or ALS inhibition. Although, both types of inhibitors induce growth arrest and photosynthesis inhibition, plant death occurs more rapidly under ALS inhibition than KARI inhibition. Carbohydrates accumulated in the leaves and roots following treatments with both inhibitors. The carbohydrate accumulation in the leaves occurred as a consequence of a decrease in sink strength. In contrast, the free amino acid content was only affected through ALS inhibition. These results indicate that although KARI and ALS inhibition block the same biosynthetic pathway and exert common effects on carbon metabolism, nitrogen metabolism is more affected via ALS than KARI inhibition. Thus, metabolic alterations in nitrogen metabolism induced through ALS inhibitors might contribute to the increased efficacy of these chemicals as herbicides.en
dc.description.sponsorshipM. Igal received a grant from the Public University of Navarre. A. Zulet and M. Gil-Monreal receive funding through fellowships from the Spanish Ministry of Education and the Public University of Navarre, respectively. This work was financially supported through grants from the Spanish Ministry of Education and Science (AGL-2010-18621).en
dc.format.mimetypeapplication/pdfen
dc.identifier.doi10.1016/j.jplph.2013.01.003
dc.identifier.issn0176-1617 (Print)
dc.identifier.issn1618-1328 (Electronic)
dc.identifier.urihttps://academica-e.unavarra.es/handle/2454/24073
dc.language.isoengen
dc.publisherElsevieren
dc.relation.ispartofJournal of Plant Physiology 170 (2013) 814–821en
dc.relation.projectIDinfo:eu-repo/grantAgreement/MICINN//AGL2010-18621/ES/en
dc.relation.publisherversionhttp://doi.org/10.1016/j.jplph.2013.01.003
dc.rights© 2013 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.subjectMode of actionen
dc.subjectHerbicideen
dc.subjectBranched-chain amino aciden
dc.subjectAcetolactate synthaseen
dc.subjectKetol-acid reductoisomeraseen
dc.titleBranched-chain amino acid biosynthesis inhibitors: herbicide efficacy is associated with an induced carbon–nitrogen imbalanceen
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
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relation.isAuthorOfPublication.latestForDiscovery0085d805-7945-48bf-994f-85bc2c88d92b

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