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Mutagenesis of cysteine 81 prevents dimerization of the APS1 subunit of ADP-glucose pyrophosphorylase and alters diurnal starch turnover in Arabidopsis thaliana leaves

hal.structure.identifierMax Planck Institute of Molecular Plant Physiology [MPI-MP]
dc.contributor.authorHÄDRICH, Nadja
hal.structure.identifierMax Planck Institute of Molecular Plant Physiology [MPI-MP]
dc.contributor.authorHENDRIKS, Janneke H.M.
hal.structure.identifierDepartment of Biology
dc.contributor.authorKÖTTING, Oliver
hal.structure.identifierMax Planck Institute of Molecular Plant Physiology [MPI-MP]
dc.contributor.authorARRIVAULT, Stéphanie
hal.structure.identifierMax Planck Institute of Molecular Plant Physiology [MPI-MP]
dc.contributor.authorFEIL, Regina
hal.structure.identifierDepartment of Biology
dc.contributor.authorZEEMAN, Samuel C.
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorGIBON, Yves
hal.structure.identifierMax Planck Institute of Molecular Plant Physiology [MPI-MP]
dc.contributor.authorSCHULZE, Waltraud X.
hal.structure.identifierMax Planck Institute of Molecular Plant Physiology [MPI-MP]
dc.contributor.authorSTITT, Mark
hal.structure.identifierMax Planck Institute of Molecular Plant Physiology [MPI-MP]
dc.contributor.authorLUNN, John E.
dc.date.issued2012
dc.identifier.issn0960-7412
dc.description.abstractEnMany plants, including Arabidopsis thaliana, retain a substantial portion of their photosynthate in leaves in the form of starch, which is remobilized to support metabolism and growth at night. ADP-glucose pyrophosphorylase (AGPase) catalyses the first committed step in the pathway of starch synthesis, the production of ADP-glucose. The enzyme is redox-activated in the light and in response to sucrose accumulation, via reversible breakage of an intermolecular cysteine bridge between the two small (APS1) subunits. The biological function of this regulatory mechanism was investigated by complementing an aps1 null mutant (adg1) with a series of constructs containing a full-length APS1 gene encoding either the wild-type APS1 protein or mutated forms in which one of the five cysteine residues was replaced by serine. Substitution of Cys81 by serine prevented APS1 dimerization, whereas mutation of the other cysteines had no effect. Thus, Cys81 is both necessary and sufficient for dimerization of APS1. Compared to control plants, the adg1/APS1C81S lines had higher levels of ADP-glucose and maltose, and either increased rates of starch synthesis or a starch-excess phenotype, depending on the daylength. APS1 protein levels were five- to tenfold lower in adg1/APS1C81S lines than in control plants. These results show that redox modulation of AGPase contributes to the diurnal regulation of starch turnover, with inappropriate regulation of the enzyme having an unexpected impact on starch breakdown, and that Cys81 may play an important role in the regulation of AGPase turnover.
dc.language.isoen
dc.publisherWiley
dc.subjectcysteine
dc.subject.enADP-glucose pyrophosphorylase
dc.subject.enArabidopsis thaliana
dc.subject.enstarch
dc.subject.ensite-directed mutagenesis
dc.subject.enthioredoxin
dc.title.enMutagenesis of cysteine 81 prevents dimerization of the APS1 subunit of ADP-glucose pyrophosphorylase and alters diurnal starch turnover in Arabidopsis thaliana leaves
dc.typeArticle de revue
dc.identifier.doi10.1111/j.1365-313X.2011.04860.x
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale
bordeaux.journalPlant Journal
bordeaux.page231-242
bordeaux.volume70
bordeaux.issue2
bordeaux.peerReviewedoui
hal.identifierhal-02644594
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02644594v1
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