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The E3 ubiquitin-ligase SEVEN IN ABSENTIA like 7 mono-ubiquitinates glyceraldehyde-3-phosphate dehydrogenase 1 isoform in vitro and is required for its nuclear localization in Arabidopsis thaliana.

hal.structure.identifierUniversidad Nacional de Rosario [Santa Fe]
dc.contributor.authorPERALTA, Diego A
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorARAYA, Alejandro
hal.structure.identifierUniversidad Nacional de Rosario [Santa Fe]
dc.contributor.authorBUSI, Maria V
hal.structure.identifierUniversidad Nacional de Rosario [Santa Fe]
dc.contributor.authorGOMEZ-CASATI, Diego F
dc.date.issued2016
dc.identifier.issn1357-2725
dc.description.abstractEnThe E3 ubiquitin-protein ligases are associated to various processes such as cell cycle control and diverse developmental pathways. Arabidopsis thaliana SEVEN IN ABSENTIA like 7, which has ubiquitin ligase activity, is located in the nucleus and cytosol and is expressed at several stages in almost all plant tissues suggesting an important role in plant functions. However, the mechanism underlying the regulation of this protein is unknown. Since we found that the SEVEN IN ABSENTIA like 7 gene expression is altered in plants with impaired mitochondria, and in plants deficient in the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase 1, we decided to study the possible interactions between both proteins as potential partners in plant signaling functions. We found that SEVEN IN ABSENTIA like 7 is able to interact in vitro with glyceraldehyde-3-phosphate dehydrogenase and that the Lys231 residue of the last is essential for this function. Following the interaction, a concomitant increase in the glyceraldehyde-3-phosphate dehydrogenase catalytic activity was observed. However, when SEVEN IN ABSENTIA like 7 was supplemented with E1 and E2 proteins to form a complete E1-E2-E3 modifier complex, we observed the mono-ubiquitination of glyceraldehyde-3-phosphate dehydrogenase 1 at the Lys76 residue and a dramatic decrease of its catalytic activity. Moreover, we found that localization of glyceraldehyde-3-phosphate dehydrogenase 1 in the nucleus is dependent on the expression SEVEN IN ABSENTIA like 7. These observations suggest that the association of both proteins might result in different biological consequences in plants either through affecting the glycolytic flux or via cytoplasm-nucleus relocation.
dc.language.isoen
dc.publisherElsevier
dc.subjectGAPC
dc.subjectUbiquitination
dc.subject.enInteraction
dc.subject.enNuclear localization
dc.subject.enSINAL7
dc.title.enThe E3 ubiquitin-ligase SEVEN IN ABSENTIA like 7 mono-ubiquitinates glyceraldehyde-3-phosphate dehydrogenase 1 isoform in vitro and is required for its nuclear localization in Arabidopsis thaliana.
dc.typeArticle de revue
dc.identifier.doi10.1016/j.biocel.2015.11.007
dc.subject.halSciences du Vivant [q-bio]/Biologie végétale
bordeaux.journalInternational Journal of Biochemistry and Cell Biology
bordeaux.page48-56
bordeaux.volume70
bordeaux.peerReviewedoui
hal.identifierhal-02634297
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-02634297v1
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