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Molecular Mechanism Underlying the Plant NRT1.1 Dual-Affinity Nitrate Transporter

机译:植物NRT1.1双亲和硝酸盐转运蛋白的分子机制

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摘要

Nitrate (NO3) is one of the most important sources of mineral nitrogen, which also serves as a key signaling molecule for plant growth and development. To cope with nitrate fluctuation in soil that varies by up to four orders of magnitude, plants have evolved high- and low-affinity nitrate transporter systems, consisting of distinct families of transporters. Interestingly, the first cloned nitrate transporter in Arabidopsis, NRT1.1 functions as a dual-affinity transporter, which can change its affinity for nitrate in response to substrate availability. Phosphorylation of a threonine residue, Thr101, switches NRT1.1 from low- to high-affinity state. Recent structural studies have unveiled that the unmodified NRT1.1 transporter works as homodimers with Thr101 located in close proximity to the dimer interface. Modification on the Thr101 residue is shown to not only decouple the dimer configuration, but also increase structural flexibility, thereby, altering the substrate affinity of NRT1.1. The structure of NRT1.1 helps establish a novel paradigm in which protein oligomerzation and posttranslational modification can synergistically expand the functional capacity of the major facilitator superfamily (MFS) transporters.
机译:硝酸盐(<数学xmlns:mml =“ http://www.w3.org/1998/Math/MathML” id =“ M1” overflow =“ scroll”> NO 3 )是最重要的矿质氮源之一,也是植物的重要信号分子增长与发展。为了应对最多四个数量级变化的土壤中硝酸盐的波动,植物已经进化出高亲和力和低亲和力的硝酸盐转运系统,包括不同的转运体家族。有趣的是,NRT1.1是拟南芥中第一个克隆的硝酸盐转运蛋白,具有双重亲和力转运蛋白的功能,可以响应底物的可用性改变其对硝酸盐的亲和力。苏氨酸残基Thr101的磷酸化将NRT1.1从低亲和力状态切换为高亲和力状态。最近的结构研究表明,未经修饰的NRT1.1转运蛋白可作为同源二聚体使用,其中Thr101位于二聚体界面附近。显示对Thr101残基的修饰不仅解偶联二聚体构型,而且增加结构柔性,从而改变NRT1.1的底物亲和力。 NRT1.1的结构有助于建立一种新的范式,其中蛋白质的寡聚和翻译后修饰可以协同扩展主要辅助超家族(MFS)转运蛋白的功能。

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