Ammonium ion transport by the AMT/Rh homolog TaAMT1;1 is stimulated by acidic pH

Research output: Contribution to journalJournal articlepeer-review

Standard

Ammonium ion transport by the AMT/Rh homolog TaAMT1;1 is stimulated by acidic pH. / Søgaard, Rikke; Alsterfjord, Magnus; Macaulay, Nanna; Zeuthen, Thomas.

In: Pflügers Archiv: European Journal of Physiology, Vol. 458, No. 4, 2009, p. 733-43.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Søgaard, R, Alsterfjord, M, Macaulay, N & Zeuthen, T 2009, 'Ammonium ion transport by the AMT/Rh homolog TaAMT1;1 is stimulated by acidic pH', Pflügers Archiv: European Journal of Physiology, vol. 458, no. 4, pp. 733-43. https://doi.org/10.1007/s00424-009-0665-z

APA

Søgaard, R., Alsterfjord, M., Macaulay, N., & Zeuthen, T. (2009). Ammonium ion transport by the AMT/Rh homolog TaAMT1;1 is stimulated by acidic pH. Pflügers Archiv: European Journal of Physiology, 458(4), 733-43. https://doi.org/10.1007/s00424-009-0665-z

Vancouver

Søgaard R, Alsterfjord M, Macaulay N, Zeuthen T. Ammonium ion transport by the AMT/Rh homolog TaAMT1;1 is stimulated by acidic pH. Pflügers Archiv: European Journal of Physiology. 2009;458(4):733-43. https://doi.org/10.1007/s00424-009-0665-z

Author

Søgaard, Rikke ; Alsterfjord, Magnus ; Macaulay, Nanna ; Zeuthen, Thomas. / Ammonium ion transport by the AMT/Rh homolog TaAMT1;1 is stimulated by acidic pH. In: Pflügers Archiv: European Journal of Physiology. 2009 ; Vol. 458, No. 4. pp. 733-43.

Bibtex

@article{c20f13109e0011debc73000ea68e967b,
title = "Ammonium ion transport by the AMT/Rh homolog TaAMT1;1 is stimulated by acidic pH",
abstract = "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.",
author = "Rikke S{\o}gaard and Magnus Alsterfjord and Nanna Macaulay and Thomas Zeuthen",
year = "2009",
doi = "10.1007/s00424-009-0665-z",
language = "English",
volume = "458",
pages = "733--43",
journal = "Pfl{\"u}gers Archiv - European Journal of Physiology",
issn = "0031-6768",
publisher = "Springer",
number = "4",

}

RIS

TY - JOUR

T1 - Ammonium ion transport by the AMT/Rh homolog TaAMT1;1 is stimulated by acidic pH

AU - Søgaard, Rikke

AU - Alsterfjord, Magnus

AU - Macaulay, Nanna

AU - Zeuthen, Thomas

PY - 2009

Y1 - 2009

N2 - 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.

AB - 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.

U2 - 10.1007/s00424-009-0665-z

DO - 10.1007/s00424-009-0665-z

M3 - Journal article

C2 - 19340454

VL - 458

SP - 733

EP - 743

JO - Pflügers Archiv - European Journal of Physiology

JF - Pflügers Archiv - European Journal of Physiology

SN - 0031-6768

IS - 4

ER -

ID: 14334795