The Dionaea muscipula Ammonium Channel DmAMT1 Provides NH4+ Uptake Associated 
with Venus Flytrap’s Prey Digestion

Scherzer, S.; Kro, E.; Kreuzer, I.; Kruse, J.; Karl, F.; von Rüden, M.; Escalante-Perez, M.; Müller, T.; Rennenberg, H.; Al-Rashcheid, K. A. S.; Neher, E.; Hedrich, R.

doi:10.1016/j.cub.2013.07.028

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The Dionaea muscipula Ammonium Channel DmAMT1 Provides NH₄⁺ Uptake Associated with Venus Flytrap’s Prey Digestion

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Neher, E.
Emeritus Group of Membrane Biophysics, MPI for Biophysical Chemistry, Max Planck Society;

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引用

Scherzer, S., Kro, E., Kreuzer, I., Kruse, J., Karl, F., von Rüden, M., Escalante-Perez, M., Müller, T., Rennenberg, H., Al-Rashcheid, K. A. S., Neher, E., & Hedrich, R. (2013). The Dionaea muscipula Ammonium Channel DmAMT1 Provides NH₄⁺ Uptake Associated with Venus Flytrap’s Prey Digestion. Current Biology, 23(17), 1649-1657. doi:10.1016/j.cub.2013.07.028.

引用: https://hdl.handle.net/11858/00-001M-0000-0015-78ED-5

要旨

Background: Ammonium transporter (AMT/MEP/Rh) superfamily members mediate ammonium uptake and retrieval. This pivotal transport system is conserved among all living organisms. For plants, nitrogen represents a macronutrient available in the soil as ammonium, nitrate, and organic nitrogen compounds. Plants living on extremely nutrient-poor soils have developed a number of adaptation mechanisms, including a carnivorous lifestyle. This study addresses the molecular nature, function, and regulation of prey-derived ammonium uptake in the Venus flytrap, Dionaea muscipula, one of the fastest active carnivores.

Results: The Dionaea muscipula ammonium transporter DmAMT1 was localized in gland complexes where its expression was upregulated upon secretion. These clusters of cells decorating the inner trap surface are engaged in (1) secretion of an acidic digestive enzyme cocktail and (2) uptake of prey-derived nutrients. Voltage clamp of Xenopus oocytes expressing DmAMT1 and membrane potential recordings with DmAMT1-expressing Dionaea glands were used to monitor and compare electrophysiological properties of DmAMT1 in vitro and in planta. DmAMT1 exhibited the hallmark biophysical properties of a NH4+-selective channel. At depolarized membrane potentials (V-m = 0), the K-m (3.2 +/- 0.3 mM) indicated a low affinity of DmAMT1 for ammonium that increased systematically with negative going voltages. Upon hyperpolarization to, e.g., -200 mV, a K-m of 0.14 +/- 0.015 mM documents the voltage-dependent shift of DmAMT1 into a NH4+ transport system of high affinity.

Conclusions: We suggest that regulation of glandular DmAMT1 and membrane potential readjustments of the endocrine cells provide for effective adaptation to varying, prey-derived ammonium sources.