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首页> 美国卫生研究院文献>Plant and Cell Physiology >A Functional EXXEK Motif is Essential for Proton Coupling and Active Glucosinolate Transport by NPF2.11
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A Functional EXXEK Motif is Essential for Proton Coupling and Active Glucosinolate Transport by NPF2.11

机译：功能性EXXEK图案对于NPF2.11的质子偶联和有效的芥子油苷运输至关重要。

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摘要

The proton-dependent oligopeptide transporter (POT/PTR) family shares a highly conserved E1X1X2E2RFXYY (E1X1X2E2R) motif across all kingdoms of life. This motif is suggested to have a role in proton coupling and active transport in bacterial homologs. For the plant POT/PTR family, also known as the NRT1/PTR family (NPF), little is known about the role of the E1X1X2E2R motif. Moreover, nothing is known about the role of the X1 and X2 residues within the E1X1X2E2R motif. We used NPF2.11—a proton-coupled glucosinolate (GLS) symporter from Arabidopsis thaliana—to investigate the role of the E1X1X2E2K motif variant in a plant NPF transporter. Using liquid chromatography–mass spectrometry (LC-MS)-based uptake assays and two-electrode voltage clamp (TEVC) electrophysiology, we demonstrate an essential role for the E1X1X2E2K motif for accumulation of substrate by NPF2.11. Our data suggest that the highly conserved E1, E2 and K residues are involved in translocation of protons, as has been proposed for the E1X1X2E2R motif in bacteria. Furthermore, we show that the two residues X1 and X2 in the E1X1X2E2[K/R] motif are conserved as uncharged amino acids in POT/PTRs from bacteria to mammals and that introducing a positive or negative charge in either position hampers the ability to overaccumulate substrate relative to the assay medium. We hypothesize that introducing a charge at X1 and X2 interferes with the function of the conserved glutamate and lysine residues of the E1X1X2E2K motif and affects the mechanism behind proton coupling.
机译：依赖质子的寡肽转运蛋白（POT / PTR）家族在所有生命王国中均具有高度保守的E1X1X2E2RFXYY（E1X1X2E2R）主题。建议该基序在细菌同源物中的质子偶联和主动转运中起作用。对于植物POT / PTR家族（也称为NRT1 / PTR家族（NPF）），对E1X1X2E2R主题的作用知之甚少。而且，关于E1X1X 2 E 2 R基序中的X1和X2残基的作用还一无所知。我们使用NPF2.11（一种来自拟南芥的质子偶联的芥子油苷（GLS）转运体）来研究E 1 X 1 X 2 的作用。植物NPF转运蛋白中的sub> E 2 K基序变体。使用基于液相色谱-质谱（LC-MS）的吸收测定法和两电极电压钳（TEVC）电生理学，我们证明了E 1 X 1 X 2 E 2 K基元通过NPF2.11积累底物。我们的数据表明，高度保守的E 1 ，E 2 和K残基与质子易位有关，正如针对E 1 X 1 X 2 E 2 R基序。此外，我们显示了E 1 X 1 X 1 和X 2 > 2 E 2 [K / R]基序在细菌到哺乳动物的POT / PTR中被保留为不带电荷的氨基酸，并且在任一位置引入正电荷或负电荷均会阻碍相对于测定培养基，底物过度积聚。我们假设在X 1 和X 2 引入电荷会干扰E 1 X <的保守的谷氨酸和赖氨酸残基的功能sub> 1 X 2 E 2 K基序，影响质子耦合的机理。

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