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首页> 外文期刊>Nature >Unsynchronised subunit motion in single trimeric sodium-coupled aspartate transporters
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Unsynchronised subunit motion in single trimeric sodium-coupled aspartate transporters

机译：三聚体钠偶联天冬氨酸转运蛋白中不同步的亚基运动

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摘要

Excitatory amino acid transporters (EAATs) are secondary transport proteins that mediate the uptake of glutamate and other amino acids. EAATs fulfil an important role in neuronal signal transmission by clearing the excitatory neurotransmitters from the synaptic cleft after depolarization of the postsynaptic neuron. An intensively studied model system for understanding the transport mechanism of EAATs is the archaeal aspartate transporter Glt_(Ph). Each subunit in the homotrimeric Glt_(Ph) supports the coupled translocation of one aspartate molecule and three Na~+ ions as well as an uncoupled flux of Cl~- ions. Recent crystal structures of Glt_(Ph) revealed three possible conformations for the subunits, but it is unclear whether the motions of individual subunits are coordinated to support transport. Here, we report the direct observation of conformational dynamics in individual Glt_(Ph) trimers embedded in the membrane by applying single-molecule fluorescence resonance energy transfer (FRET). By analysing the transporters in a lipid bilayer instead of commonly used detergent micelles, we achieve conditions that approximate the physiologically relevant ones. From the kinetics of FRET level transitions we conclude that the three Glt_(Ph) subunits undergo conformational changes stochastically and independently of each other.
机译：兴奋性氨基酸转运蛋白（EAAT）是介导谷氨酸和其他氨基酸摄取的二级转运蛋白。 EAAT通过使突触后神经元去极化后清除突触间隙中的兴奋性神经递质，从而在神经元信号传递中发挥重要作用。深入研究的用于理解EAAT转运机制的模型系统是古天冬氨酸转运蛋白Glt_（Ph）。同型三聚体Glt_（Ph）中的每个亚基都支持一个天冬氨酸分子和三个Na〜+离子的偶联易位以及Cl〜-离子的未偶联通量。 Glt_（Ph）的最新晶体结构揭示了亚基的三个可能构象，但尚不清楚单个亚基的运动是否经过协调以支持转运。在这里，我们报告通过应用单分子荧光共振能量转移（FRET）直接观察嵌入膜中的各个Glt_（Ph）三聚体的构象动力学。通过分析脂质双层中的转运蛋白而不是常用的清洁剂胶束，我们获得了与生理学相关的条件近似的条件。从FRET水平跃迁的动力学，我们得出结论，三个Glt_（Ph）亚基随机且彼此独立地经历构象变化。

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  • 来源
    《Nature》 |2013年第7469期|119-123|共5页
  • 作者

    Guus B. Erkens; Inga Haenelt; Joris M. H. Goudsmits; Dirk Jan Slotboom; Antoine M. van Oijen;

  • 作者单位

    University of Groningen, Zemike Institute for Advanced Materials, Nijenborgh 4,9747 AG Groningen,The Netherlands;

    University of Groningen, Zemike Institute for Advanced Materials, Nijenborgh 4,9747 AG Groningen,The Netherlands,University of Groningen, Groningen Biomolecular Science and Biotechnology Institute, Nijenborgh 4,9747 AG Groningen, The Netherlands,Goethe-University Frankfurt, Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Max-von-Laue-Strasse 9,60438 Frankfurt am Main, Germany;

    University of Groningen, Zemike Institute for Advanced Materials, Nijenborgh 4,9747 AG Groningen,The Netherlands;

    University of Groningen, Zemike Institute for Advanced Materials, Nijenborgh 4,9747 AG Groningen,The Netherlands,University of Groningen, Groningen Biomolecular Science and Biotechnology Institute, Nijenborgh 4,9747 AG Groningen, The Netherlands,University of Groningen, Centre for Synthetic Biology, Nijenborgh 4,9747 AG Groningen, The Netherlands;

    University of Groningen, Zemike Institute for Advanced Materials, Nijenborgh 4,9747 AG Groningen,The Netherlands,University of Groningen, Groningen Biomolecular Science and Biotechnology Institute, Nijenborgh 4,9747 AG Groningen, The Netherlands,University of Groningen, Centre for Synthetic Biology, Nijenborgh 4,9747 AG Groningen, The Netherlands;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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