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      Transport Function of Rice Amino Acid Permeases (AAPs).

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          Abstract

          The transport function of four rice (Oryza sativa) amino acid permeases (AAPs), OsAAP1 (Os07g04180), OsAAP3 (Os06g36180), OsAAP7 (Os05g34980) and OsAAP16 (Os12g08090), was analyzed by expression in Xenopus laevis oocytes and electrophysiology. OsAAP1, OsAAP7 and OsAAP16 functioned, similarly to Arabidopsis AAPs, as general amino acid permeases. OsAAP3 had a distinct substrate specificity compared with other rice or Arabidopsis AAPs. OsAAP3 transported the basic amino acids lysine and arginine well but selected against aromatic amino acids. The transport of basic amino acids was further analyzed for OsAAP1 and OsAAP3, and the results support the transport of both neutral and positively charged forms of basic amino acids by the rice AAPs. Cellular localization using the tandem enhanced green fluorescent protein (EGFP)-red fluorescent protein (RFP) reporter pHusion showed that OsAAP1 and OsAAP3 localized to the plasma membrane after transient expression in onion epidermal cells or stable expression in Arabidopsis.

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          Author and article information

          Journal
          Plant Cell Physiol.
          Plant & cell physiology
          Oxford University Press (OUP)
          1471-9053
          0032-0781
          Jul 2015
          : 56
          : 7
          Affiliations
          [1 ] Department of Plant Biology, University of Minnesota, St. Paul, MN 55108, USA.
          [2 ] Department of Plant Biology, University of Minnesota, St. Paul, MN 55108, USA jward@umn.edu.
          Article
          pcv053
          10.1093/pcp/pcv053
          25907566
          559eca97-3ec3-40ce-8676-00ed0f0354ce
          History

          Xenopus oocytes,amino acid transporters,electrophysiology,rice AAPs

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