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dc.contributor.authorPlessis, Anne
dc.contributor.authorBoudet, J
dc.contributor.authorGaudin, J-C
dc.contributor.authorMerlino, M
dc.contributor.authorDardevet, M
dc.contributor.authorPerrochon, S
dc.contributor.authorAlvarez, D
dc.contributor.authorRisacher, T
dc.contributor.authorMartre, P
dc.contributor.authorRavel, C
dc.date.accessioned2018-12-06T16:34:09Z
dc.date.issued2018-11-16
dc.identifier.issn0960-7412
dc.identifier.issn1365-313X
dc.identifier.urihttp://hdl.handle.net/10026.1/12997
dc.description.abstract

<jats:title>Summary</jats:title><jats:p>The quality of wheat grain is mainly determined by the quantity and composition of its grain storage proteins (<jats:styled-content style="fixed-case">GSP</jats:styled-content>s). Grain storage proteins consist of low‐ and high‐molecular‐weight glutenins (<jats:styled-content style="fixed-case">LMW</jats:styled-content>‐<jats:styled-content style="fixed-case">GS</jats:styled-content> and <jats:styled-content style="fixed-case">HMW</jats:styled-content>‐<jats:styled-content style="fixed-case">GS</jats:styled-content>, respectively) and gliadins. The synthesis of these proteins is essentially regulated at the transcriptional level and by the availability of nitrogen and sulfur. The regulation network has been extensively studied in barley where <jats:styled-content style="fixed-case">BLZ</jats:styled-content>1 and <jats:styled-content style="fixed-case">BLZ</jats:styled-content>2, members of the basic leucine zipper (<jats:styled-content style="fixed-case">bZIP</jats:styled-content>) family, activate the synthesis of hordeins. To date, in wheat, only the ortholog of <jats:styled-content style="fixed-case">BLZ</jats:styled-content>2, Storage Protein Activator (<jats:styled-content style="fixed-case">SPA</jats:styled-content>), has been identified as playing a major role in the regulation of <jats:styled-content style="fixed-case">GSP</jats:styled-content> synthesis. Here, the ortholog of <jats:styled-content style="fixed-case">BLZ</jats:styled-content>1, named SPA Heterodimerizing Protein (<jats:styled-content style="fixed-case">SHP</jats:styled-content>), was identified and its involvement in the transcriptional regulation of the genes coding for <jats:styled-content style="fixed-case">GSP</jats:styled-content>s was analyzed. In gel mobility shift assays, <jats:styled-content style="fixed-case">SHP</jats:styled-content> binds <jats:italic>cis</jats:italic>‐motifs known to bind to <jats:styled-content style="fixed-case">bZIP</jats:styled-content> family transcription factors in <jats:styled-content style="fixed-case">HMW</jats:styled-content>‐<jats:styled-content style="fixed-case">GS</jats:styled-content> and <jats:styled-content style="fixed-case">LMW</jats:styled-content>‐<jats:styled-content style="fixed-case">GS</jats:styled-content> promoters. Moreover, we showed by transient expression assays in wheat endosperm that <jats:styled-content style="fixed-case">SHP</jats:styled-content> acts as a repressor of the activity of these gene promoters. This result was confirmed in transgenic lines overexpressing <jats:italic><jats:styled-content style="fixed-case">SHP</jats:styled-content></jats:italic>, which were grown with low and high nitrogen supply. The phenotype of <jats:italic><jats:styled-content style="fixed-case">SHP</jats:styled-content></jats:italic>‐overexpressing lines showed a lower quantity of both <jats:styled-content style="fixed-case">LMW</jats:styled-content>‐<jats:styled-content style="fixed-case">GS</jats:styled-content> and <jats:styled-content style="fixed-case">HMW</jats:styled-content>‐<jats:styled-content style="fixed-case">GS</jats:styled-content>, while the quantity of gliadin was unchanged, whatever the nitrogen availability. Thus, the gliadin/glutenin ratio was increased, which suggests that gliadin and glutenin genes may be differently regulated.</jats:p>

dc.format.extent858-871
dc.format.mediumPrint-Electronic
dc.languageen
dc.language.isoen
dc.publisherWiley
dc.subjectSPA Heterodimerizing Protein
dc.subjectbZIP transcription factor
dc.subjectgluten
dc.subjectstorage proteins
dc.subjectwheat (Triticum aestivum L.)
dc.subjectBasic-Leucine Zipper Transcription Factors
dc.subjectGene Expression Regulation, Plant
dc.subjectGlutens
dc.subjectPlant Proteins
dc.subjectPlants, Genetically Modified
dc.subjectProtein Multimerization
dc.subjectTriticum
dc.titleThe bZIP transcription factor SPA Heterodimerizing Protein represses glutenin synthesis in Triticum aestivum
dc.typejournal-article
dc.typeJournal Article
dc.typeResearch Support, Non-U.S. Gov't
plymouth.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/30444293
plymouth.issue5
plymouth.volume97
plymouth.publication-statusPublished
plymouth.journalPlant Journal
dc.identifier.doi10.1111/tpj.14163
plymouth.organisational-group/Plymouth
plymouth.organisational-group/Plymouth/Faculty of Science and Engineering
plymouth.organisational-group/Plymouth/Faculty of Science and Engineering/School of Biological and Marine Sciences
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA
plymouth.organisational-group/Plymouth/REF 2021 Researchers by UoA/UoA06 Agriculture, Veterinary and Food Science
plymouth.organisational-group/Plymouth/Users by role
plymouth.organisational-group/Plymouth/Users by role/Academics
dc.publisher.placeEngland
dcterms.dateAccepted2018-10-31
dc.rights.embargodate2019-11-16
dc.identifier.eissn1365-313X
dc.rights.embargoperiodNot known
rioxxterms.versionofrecord10.1111/tpj.14163
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2018-11-16
rioxxterms.typeJournal Article/Review


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