Suppr超能文献

植物NRT1.1双亲和性硝酸盐转运体的分子机制

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

作者信息

Sun Ji, Zheng Ning

机构信息

Department of Pharmacology, University of Washington Seattle, WA, USA.

Department of Pharmacology, University of WashingtonSeattle, WA, USA; Howard Hughes Medical Institute, University of WashingtonSeattle, WA, USA.

出版信息

Front Physiol. 2015 Dec 18;6:386. doi: 10.3389/fphys.2015.00386. eCollection 2015.

Abstract

Nitrate ([Formula: see text]) 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.

摘要

硝酸盐([化学式:见原文])是矿质氮最重要的来源之一,也是植物生长发育的关键信号分子。为应对土壤中变化幅度高达四个数量级的硝酸盐波动,植物进化出了高亲和性和低亲和性硝酸盐转运系统,这些系统由不同的转运蛋白家族组成。有趣的是,拟南芥中首个被克隆的硝酸盐转运蛋白NRT1.1具有双亲和性转运功能,它能根据底物的可利用性改变对硝酸盐的亲和力。苏氨酸残基Thr101的磷酸化会使NRT1.1从低亲和状态转变为高亲和状态。最近的结构研究表明,未修饰的NRT1.1转运蛋白以同二聚体形式发挥作用,Thr101位于靠近二聚体界面的位置。Thr101残基的修饰不仅会使二聚体结构解耦,还会增加结构灵活性,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模式,即蛋白质寡聚化和翻译后修饰可以协同扩展主要转运子超家族(MFS)转运蛋白的功能能力。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cb70/4683204/8eed61ae8e05/fphys-06-00386-g0001.jpg

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验