Linked Life Data

11959905

Source:http://linkedlifedata.com/resource/pubmed/id/11959905

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pubmed-article:11959905pubmed:dateCreated2002-5-1lld:pubmed
pubmed-article:11959905pubmed:abstractTextPlant HKT proteins comprise a family of cation transporters together with prokaryotic KtrB, TrkH, and KdpA transporter subunits and fungal Trk proteins. These transporters contain four loop domains in one polypeptide with a proposed distant homology to K(+) channel selectivity filters. Functional expression in yeast and Xenopus oocytes revealed that wheat HKT1 mediates Na(+)-coupled K(+) transport. Arabidopsis AtHKT1, however, transports only Na(+) in eukaryotic expression systems. To understand the molecular basis of this difference we constructed a series of AtHKT1/HKT1 chimeras and introduced point mutations to AtHKT1 and wheat HKT1 at positions predicted to be critical for K(+) selectivity. A single-point mutation, Ser-68 to glycine, was sufficient to restore K(+) permeability to AtHKT1. The reverse mutation in HKT1, Gly-91 to serine, abrogated K(+) permeability. This glycine in P-loop A of AtHKT1 and HKT1 can be modeled as the first glycine of the K(+) channel selectivity filter GYG motif. The importance of such filter glycines for K(+) selectivity was confirmed by interconversion of Ser-88 and Gly-88 in the rice paralogues OsHKT1 and OsHKT2. Surprisingly, all HKT homologues known from dicots have a serine at the filter position in P-loop A, suggesting that these proteins function mainly as Na(+) transporters in plants and that Na(+)/K(+) symport in HKT proteins is associated with a glycine in the filter residue. These data provide experimental evidence that the glycine residues in selectivity filters of HKT proteins are structurally related to those of K(+) channels.lld:pubmed
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pubmed-article:11959905pubmed:authorpubmed-author:GoshimaShinob...lld:pubmed
pubmed-article:11959905pubmed:authorpubmed-author:UozumiNobuyuk...lld:pubmed
pubmed-article:11959905pubmed:authorpubmed-author:BakkerEvert...lld:pubmed
pubmed-article:11959905pubmed:authorpubmed-author:MäserPascalPlld:pubmed
pubmed-article:11959905pubmed:authorpubmed-author:HosooYoshihir...lld:pubmed
pubmed-article:11959905pubmed:authorpubmed-author:HorieTomoakiTlld:pubmed
pubmed-article:11959905pubmed:authorpubmed-author:EckelmanBrend...lld:pubmed
pubmed-article:11959905pubmed:authorpubmed-author:YamadaKatsuyu...lld:pubmed
pubmed-article:11959905pubmed:authorpubmed-author:YoshidaKazuya...lld:pubmed
pubmed-article:11959905pubmed:authorpubmed-author:ShinmyoAtsuhi...lld:pubmed
pubmed-article:11959905pubmed:authorpubmed-author:OikiShigetosh...lld:pubmed
pubmed-article:11959905pubmed:authorpubmed-author:SchroederJuli...lld:pubmed
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pubmed-article:11959905pubmed:dateRevised2010-9-14lld:pubmed
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