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  <Article>
    <Journal>
      <PublisherName>MDPI</PublisherName>
      <JournalTitle>Acta Medica Okayama</JournalTitle>
      <Issn>2223-7747</Issn>
      <Volume>9</Volume>
      <Issue>1</Issue>
      <PubDate PubStatus="ppublish">
        <Year>2019</Year>
        <Month/>
      </PubDate>
    </Journal>
    <ArticleTitle>Expression and Ion Transport Activity of Rice OsHKT1;1 Variants</ArticleTitle>
    <FirstPage LZero="delete">16</FirstPage>
    <LastPage/>
    <Language>EN</Language>
    <AuthorList>
      <Author>
        <FirstName EmptyYN="N">Shahin</FirstName>
        <LastName>Imran</LastName>
        <Affiliation>Institute of Plant Science and Resources, Okayama University</Affiliation>
      </Author>
      <Author>
        <FirstName EmptyYN="N">Tomoaki</FirstName>
        <LastName>Horie</LastName>
        <Affiliation>Division of Applied Biology, Faculty of the Textile Science and Technology, Shinshu University</Affiliation>
      </Author>
      <Author>
        <FirstName EmptyYN="N">Maki</FirstName>
        <LastName>Katsuhara</LastName>
        <Affiliation>Institute of Plant Science and Resources, Okayama University</Affiliation>
      </Author>
    </AuthorList>
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    <Abstract>OsHKT1;1 in rice, belongs to the high-affinity K+ Transporter family, has been found to be involved in salt tolerance. OsHKT1;1 in japonica rice (Nipponbare) produces mRNA variants, but their functions remain elusive. In salt tolerant rice, Pokkali, eight OsHKT1;1 variants (V1-V8) were identified in addition to the full-length OsHKT1;1 (FL) cDNA. Absolute quantification by qPCR revealed that accumulation of OsHKT1;1-FL mRNA is minor in contrast to that of OsHKT1;1-V1, -V2, -V4, and -V7 mRNAs, all of which are predominant in shoots, while only V1 and V7 mRNAs are predominant in roots. Two electrode voltage clamp (TEVC) experiments using Xenopus laevis oocytes revealed that oocytes-expressing OsHKT1;1-FL from Pokkali exhibited inward-rectified currents in the presence of 96 mM Na+ as reported previously. Further TEVC analyses indicated that six of eight OsHKT1;1 variants elicited currents in a Na+ or a K+ bath solution. OsHKT1;1-V6 exhibited a similar inward rectification to the FL protein. Contrastingly, however, the rests mediated bidirectional currents in both Na+ and K+ bath solutions. These data suggest possibilities that novel mechanisms regulating the transport activity of OsHKT1;1 might exist, and that OsHKT1;1 variants might also carry out distinct physiological roles either independently or in combination with OsHKT1;1-FL.</Abstract>
    <CoiStatement>No potential conflict of interest relevant to this article was reported.</CoiStatement>
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      <Object Type="keyword">
        <Param Name="value">rice</Param>
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        <Param Name="value">salt tolerance</Param>
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        <Param Name="value">Na+ transport</Param>
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        <Param Name="value">K+ transport</Param>
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      <Object Type="keyword">
        <Param Name="value">mRNA variants</Param>
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    <ReferenceList/>
  </Article>
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