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Pflugers Arch
2009 Aug 01;4584:733-43. doi: 10.1007/s00424-009-0665-z.
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Ammonium ion transport by the AMT/Rh homolog TaAMT1;1 is stimulated by acidic pH.
Søgaard R
,
Alsterfjord M
,
Macaulay N
,
Zeuthen T
.
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It is unclear how ammonia is transported by proteins from the Amt/Mep/Rh superfamily. We investigated this for the ammonium transporter TaAMT1;1 from wheat expressed in Xenopus oocytes by two-electrode voltage clamp and radio-labeled uptakes. Inward currents were activated by NH (4) (+) or methylammonium ions (MeA(+)). Importantly, currents increased fivefold when the external pH was decreased from 7.4 to 5.5; this type of pH dependence is unique and is a strong indication of NH (4) (+) or MeA(+) transport. This was confirmed by the close correlation between the uptake of radio-labeled MeA(+) and MeA(+)-induced currents. Homology models of members of the Amt/Mep/Rh superfamily exhibited major divergences in their cytoplasmic regions. A point mutation in this region of TaAMT1;1 abolished the pH sensitivity and decreased the apparent affinities for NH (4) (+) and MeA(+). We suggest a model where NH (4) (+) is transported as NH(3) and H(+) via separate pathways but the latter two recombine before leaving the protein.
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