水通道蛋白与叶绿体膜通透性

N. Eckardt
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引用次数: 2

摘要

水通道蛋白是一种固有的膜蛋白,已知可促进膜水运输,存在于大多数生物体中(Agre, 2004)。它们在植物中构成了一个大家族:拟南芥、水稻和玉米,每种都有35种不同的水通道蛋白。这些最初被分为四个亚家族,主要基于定位的明显模式:质膜内在蛋白(PIPs), tono质体内在蛋白(TIPs),结节样内在膜蛋白(存在于大豆根瘤的类细菌周围膜中),以及内质网中发现的小的基本内在蛋白。然而,这种分类有些误导,因为已经在细胞器膜上发现了PIP水通道蛋白,而在质膜上发现了一些TIP水通道蛋白(Kaldenhoff等人,2007;Maurel, 2007)。最近的研究表明,除了水的运动,水通道蛋白还可能跨膜运输其他生理上重要的分子,包括CO2、h2o2、nh3 / nh41、硼和硅,因此可能参与植物的许多基本过程,如养分获取、光合作用和胁迫反应。然而,直接测量通过水通道蛋白通道的运输,并梳理出这些分子在运输中的直接作用和与水运输相关的可能的间接影响,已被证明是非常困难的。Uehlein等人(648-657页)表明,水通道蛋白Nt AQP1定位于烟草的叶绿体内膜和质膜,并提供证据表明,它促进二氧化碳进入叶绿体的运输,影响二氧化碳的固定和光合作用。Nt AQP1在叶绿体内膜和质膜上的亚细胞定位是通过免疫印迹分析、免疫金标记的电镜和绿色荧光蛋白融合的荧光显微镜来确定的。作者利用RNA干扰技术研究了AQP1在膜对水和co2渗透中的作用
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Aquaporins and Chloroplast Membrane Permeability
Aquaporins are intrinsic membrane proteins known to facilitate membrane water transport and are found in most living organisms (Agre, 2004). They comprise a large family in plants: Arabidopsis, rice, and maize each have ;35 different aquaporins. These initially were categorized into four subfamilies, largely based on apparent patterns of localization: plasma membrane intrinsic proteins (PIPs), tonoplast intrinsic proteins (TIPs), Nodulin26-like intrinsic membrane proteins, present in the peribacteroid membrane ofsoybean rootnodules, and small basic intrinsic proteins, found in the endoplasmic reticulum. However, this classification is somewhat misleading, as PIP aquaporins have been identified in organellar membranes and some TIP aquaporins in the plasma membrane (reviewed in Kaldenhoff et al., 2007; Maurel, 2007). Recent work has suggested that, in addition to water movement, aquaporins might transport other physiologically important molecules across membranes, including CO2 ,H 2O2 ,N H 3/NH4 1 , boron, and silicon, and therefore may be involved in a number of fundamental processes in plants, such as nutrient acquistion, photosynthesis, and stress responses. However, measuring transport via aquaporin channels directly and teasing apart a direct role in transport of these molecules and possible indirect affects associated with water transport has proven to be exceptionally difficult. Uehlein et al. (pages 648–657) show that the aquaporin Nt AQP1 is localized to the inner chloroplast membrane and the plasma membrane in tobacco and present evidence that it facilitates transport of CO2 into the chloroplast and impacts CO2 fixation and photosynthesis. Subcellular localization of Nt AQP1 to the inner chloroplast membrane and plasmamembrane was determined by immunblot analysis, electron microscopy using immungold labeling, and fluorescence microscopy using a green fluorescent protein fusion. The authors investigated AQP1 function in membrane permeability to water and CO2using RNA interference
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