Agp2, a Member of the Yeast Amino Acid Permease Family, Positively Regulates Polyamine Transport at the Transcriptional Level

Handle URI:
http://hdl.handle.net/10754/325318
Title:
Agp2, a Member of the Yeast Amino Acid Permease Family, Positively Regulates Polyamine Transport at the Transcriptional Level
Authors:
Aouida, Mustapha ( 0000-0001-7945-5320 ) ; Texeira, Marta Rubio; Thevelein, Johan M.; Poulin, Richard; Ramotar, Dindial
Abstract:
Agp2 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.
KAUST Department:
Center for Desert Agriculture
Citation:
Aouida 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.
Publisher:
Public Library of Science
Journal:
PLoS ONE
Issue Date:
3-Jun-2013
DOI:
10.1371/journal.pone.0065717
PubMed ID:
23755272
PubMed Central ID:
PMC3670898
Type:
Article
ISSN:
19326203
Appears in Collections:
Articles; Center for Desert Agriculture

Full metadata record

DC FieldValue Language
dc.contributor.authorAouida, Mustaphaen
dc.contributor.authorTexeira, Marta Rubioen
dc.contributor.authorThevelein, Johan M.en
dc.contributor.authorPoulin, Richarden
dc.contributor.authorRamotar, Dindialen
dc.date.accessioned2014-08-27T09:46:43Zen
dc.date.available2014-08-27T09:46:43Zen
dc.date.issued2013-06-03en
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.en
dc.identifier.issn19326203en
dc.identifier.pmid23755272en
dc.identifier.doi10.1371/journal.pone.0065717en
dc.identifier.urihttp://hdl.handle.net/10754/325318en
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.en
dc.language.isoenen
dc.publisherPublic Library of Scienceen
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.en
dc.rightsArchived with thanks to PLoS ONEen
dc.subjectcarrier proteinen
dc.subjecthexoseen
dc.subjectmutant proteinen
dc.subjectnucleosideen
dc.subjectpermeaseen
dc.subjectpolyamineen
dc.subjectprotein Agp2en
dc.subjectprotein Dur3en
dc.subjectprotein HNM1en
dc.subjectprotein Sam3en
dc.subjectunclassified drugen
dc.subjectamine transporten
dc.subjectcell membraneen
dc.subjectcontrolled studyen
dc.subjectDUR3 geneen
dc.subjectenzyme analysisen
dc.subjectenzyme localizationen
dc.subjectenzyme regulationen
dc.subjectgeneen
dc.subjectgene expression regulationen
dc.subjectgenetic transcriptionen
dc.subjectmicroarray analysisen
dc.subjectprotein familyen
dc.subjectSaccharomyces cerevisiaeen
dc.subjectSAM3 geneen
dc.subjectSKY1 geneen
dc.subjectSaccharomyces cerevisiaeen
dc.titleAgp2, a Member of the Yeast Amino Acid Permease Family, Positively Regulates Polyamine Transport at the Transcriptional Levelen
dc.typeArticleen
dc.contributor.departmentCenter for Desert Agricultureen
dc.identifier.journalPLoS ONEen
dc.identifier.pmcidPMC3670898en
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionLaboratory of Molecular Cell Biology, Institute of Botany and Microbiology, Leuven, Belgiumen
dc.contributor.institutionDepartment of Molecular Microbiology, Flanders Institute of Biotechnology, Flanders, Belgiumen
dc.contributor.institutionDepartment of Molecular Biology, Medical Biochemistry and Pathology, Laval University Quebec, Canadaen
dc.contributor.institutionMaisonneuve-Rosemont Hospital, Research Center, University of Montreal, Immunology and Oncology, Montreal, Canadaen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorAouida, Mustaphaen

Related articles on PubMed

All Items in KAUST are protected by copyright, with all rights reserved, unless otherwise indicated.