Aquaporin homologues in plants and mammals transport ammonia

Thomas P. Jahn, Anders L.B. Møller, Thomas Zeuthen(University of Copenhagen), Lars Holm(University of Copenhagen), Dan A. Klærke(University of Copenhagen), Brigitte Mohsin(Max Planck Institute of Biophysics), Werner Kühlbrandt(Max Planck Institute of Biophysics), Jan K. Schjøerring
FEBS Letters
August 12, 2004
Cited by 342Open Access
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Abstract

Using functional complementation and a yeast mutant deficient in ammonium (NH4+) transport (Deltamep1-3), three wheat (Triticum aestivum) TIP2 aquaporin homologues were isolated that restored the ability of the mutant to grow when 2 mM NH4+ was supplied as the sole nitrogen source. When expressed in Xenopus oocytes, TaTIP2;1 increased the uptake of NH4+ analogues methylammonium and formamide. Furthermore, expression of TaTIP2;1 increased acidification of the oocyte-bathing medium containing NH4+ in accordance with NH3 diffusion through the aquaporin. Homology modeling of TaTIP2;1 in combination with site directed mutagenesis suggested a new subgroup of NH3-transporting aquaporins here called aquaammoniaporins. Mammalian AQP8 sharing the aquaammoniaporin signature also complemented NH4+ transport deficiency in yeast.


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