Suppressor mutations in the Glutamine Dumper1 protein dissociate disturbance in amino acid transport from other characteristics of the Gdu1D phenotype

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dc.contributor.authorYu, Shien
dc.contributor.authorPratelli, Rejaneen
dc.contributor.authorDenbow, Cynthia J.en
dc.contributor.authorPilot, Guillaumeen
dc.contributor.departmentSchool of Plant and Environmental Sciencesen
dc.date.accessioned2019-04-30T12:45:22Zen
dc.date.available2019-04-30T12:45:22Zen
dc.date.issued2015-08-04en
dc.description.abstractIntracellular amino acid transport across plant membranes is critical for metabolic pathways which are often split between different organelles. In addition, transport of amino acids across the plasma membrane enables the distribution of organic nitrogen through the saps between leaves and developing organs. Amino acid importers have been studied for more than two decades, and their role in this process is well-documented. While equally important, amino acid exporters are not well-characterized. The over-expression of GDU1, encoding a small membrane protein with one transmembrane domain, leads to enhancement of amino acid export by Arabidopsis cells, glutamine secretion at the leaf margin, early senescence and size reduction of the plant, possibly caused by the stimulation of amino acid exporter(s). Previous work reported the identification of suppressor mutations of the GDU1 over-expression phenotype, which affected the GDU1 and LOG2 genes, the latter encoding a membrane-bound ubiquitin ligase interacting with GDU1. The present study focuses on the characterization of three additional suppressor mutations affecting GDU1. Size, phenotype, glutamine transport and amino acid tolerance were recorded for recapitulation plants and over-expressors of mutagenized GDU1 proteins. Unexpectedly, the over-expression of most mutated GDU1 led to plants with enhanced amino acid export, but failing to display secretion of glutamine and size reduction. The results show that the various effects triggered by GDU1 over-expression can be dissociated from one another by mutagenizing specific residues. The fact that these residues are not necessarily conserved suggests that the diverse biochemical properties of the GDU1 protein are not only born by the characterized transmembrane and VIMAG domains. These data provide a better understanding of the structure/function relationships of GDU1 and may enable modifying amino acid export in plants without detrimental effects on plant fitness.en
dc.description.notesThis work was supported by the National Science Foundation (MCB1052048 to GP).en
dc.description.sponsorshipNational Science Foundation [MCB1052048]en
dc.format.mimetypeapplication/pdfen
dc.identifier.doihttps://doi.org/10.3389/fpls.2015.00593en
dc.identifier.eissn1664-462Xen
dc.identifier.other593en
dc.identifier.pmid26300894en
dc.identifier.urihttp://hdl.handle.net/10919/89256en
dc.identifier.volume6en
dc.language.isoenen
dc.publisherFrontiersen
dc.rightsCreative Commons Attribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectArabidopsisen
dc.subjectsuppressor screeningen
dc.subjectethyl methanesulfonateen
dc.subjectstructure-functionen
dc.subjectamino acid transporteren
dc.subjectglutamine transporten
dc.titleSuppressor mutations in the Glutamine Dumper1 protein dissociate disturbance in amino acid transport from other characteristics of the Gdu1D phenotypeen
dc.title.serialFrontiers In Plant Scienceen
dc.typeArticle - Refereeden
dc.type.dcmitypeTexten

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