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dc.contributor.authorAouida, Mustapha
dc.contributor.authorTexeira, Marta Rubio
dc.contributor.authorThevelein, Johan M.
dc.contributor.authorPoulin, Richard
dc.contributor.authorRamotar, Dindial
dc.date.accessioned2014-08-27T09:46:43Z
dc.date.available2014-08-27T09:46:43Z
dc.date.issued2013-06-03
dc.identifier.citationAouida M, Texeira MR, Thevelein JM, Poulin R, Ramotar D (2013) Agp2, a Member of the Yeast Amino Acid Permease Family, Positively Regulates Polyamine Transport at the Transcriptional Level. PLoS ONE 8: e65717. doi:10.1371/journal.pone.0065717.
dc.identifier.issn19326203
dc.identifier.pmid23755272
dc.identifier.doi10.1371/journal.pone.0065717
dc.identifier.urihttp://hdl.handle.net/10754/325318
dc.description.abstractAgp2 is a plasma membrane protein of the Saccharomyces cerevisiae amino acid transporter family, involved in high-affinity uptake of various substrates including L-carnitine and polyamines. The discovery of two high affinity polyamine permeases, Dur3 and Sam3, prompted us to investigate whether Agp2 directly transports polyamines or acts instead as a regulator. Herein, we show that neither dur3? nor sam3? single mutant is defective in polyamine transport, while the dur3? sam3? double mutant exhibits a sharp decrease in polyamine uptake and an increased resistance to polyamine toxicity similar to the agp2? mutant. Studies of Agp2 localization indicate that in the double mutant dur3? sam3?, Agp2-GFP remains plasma membrane-localized, even though transport of polyamines is strongly reduced. We further demonstrate that Agp2 controls the expression of several transporter genes including DUR3 and SAM3, the carnitine transporter HNM1 and several hexose, nucleoside and vitamin permease genes, in addition to SKY1 encoding a SR kinase that positively regulates low-affinity polyamine uptake. Furthermore, gene expression analysis clearly suggests that Agp2 is a strong positive regulator of additional biological processes. Collectively, our data suggest that Agp2 might respond to environmental cues and thus regulate the expression of several genes including those involved in polyamine transport. © 2013 Aouida et al.
dc.language.isoen
dc.publisherPublic Library of Science (PLoS)
dc.rightsThis is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
dc.rightsArchived with thanks to PLoS ONE
dc.subjectcarrier protein
dc.subjecthexose
dc.subjectmutant protein
dc.subjectnucleoside
dc.subjectpermease
dc.subjectpolyamine
dc.subjectprotein Agp2
dc.subjectprotein Dur3
dc.subjectprotein HNM1
dc.subjectprotein Sam3
dc.subjectunclassified drug
dc.subjectamine transport
dc.subjectcell membrane
dc.subjectcontrolled study
dc.subjectDUR3 gene
dc.subjectenzyme analysis
dc.subjectenzyme localization
dc.subjectenzyme regulation
dc.subjectgene
dc.subjectgene expression regulation
dc.subjectgenetic transcription
dc.subjectmicroarray analysis
dc.subjectprotein family
dc.subjectSaccharomyces cerevisiae
dc.subjectSAM3 gene
dc.subjectSKY1 gene
dc.subjectSaccharomyces cerevisiae
dc.titleAgp2, a Member of the Yeast Amino Acid Permease Family, Positively Regulates Polyamine Transport at the Transcriptional Level
dc.typeArticle
dc.contributor.departmentDesert Agriculture Initiative
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.identifier.journalPLoS ONE
dc.identifier.pmcidPMC3670898
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionLaboratory of Molecular Cell Biology, Institute of Botany and Microbiology, Leuven, Belgium
dc.contributor.institutionDepartment of Molecular Microbiology, Flanders Institute of Biotechnology, Flanders, Belgium
dc.contributor.institutionDepartment of Molecular Biology, Medical Biochemistry and Pathology, Laval University Quebec, Canada
dc.contributor.institutionMaisonneuve-Rosemont Hospital, Research Center, University of Montreal, Immunology and Oncology, Montreal, Canada
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)
kaust.personAouida, Mustapha
refterms.dateFOA2018-06-13T14:57:13Z


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