Isolation and functional analysis of the glycerol permease activity of two new nodulin-like intrinsic proteins from salt stressed roots of the halophyte Atriplex nummularia
Isolation and functional analysis of the glycerol permease activity of two new nodulin-like intrinsic proteins from salt stressed roots of the halophyte Atriplex nummularia
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DOI：
10.1016/j.plantsci.2003.11.001
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发表时间：
2004-03-01
期刊：
影响因子：
5.2
通讯作者：
Ramos, J
中科院分区：
文献类型：
--
作者：
Cabello-Hurtado, F;Ramos, J
我们已经分离和表征转录的两个主要的内在蛋白（MIP），AnNIP 1; 1和AnNIP 1;2，盐胁迫下的盐生植物滨藜根。保守的氨基酸和系统发育分析，这些MIPs聚类到植物nodulin样内在蛋白（NIP）的亚组。通过在酵母中异源表达这两种蛋白质的功能表征证实了它们转运甘油的能力。表达功能性AnNIP 1：1和AnNIP 1：2的fps 1 Δ酵母突变体显示出增加的甘油摄取，以及与其甘油通透酶活性一致的细胞内和细胞外甘油含量。AnNIP蛋白在酵母中的正确功能表达需要去除这两种蛋白质的独特亲水性N-末端结构域，这并不表明是必要的，它们的运输活动。(C)2003爱思唯尔爱尔兰有限公司保留所有权利。
We have isolated and characterized transcripts for two major intrinsic proteins (MIPs), AnNIP1; 1 and AnNIP1;2, from salt stressed roots of the halophyte Atriplex nummularia. Conserved amino acids and phylogenetic analysis of these MIPs clusters them into the plant nodulin-like intrinsic protein (NIP) subgroup. Functional characterization by heterologous expression of both proteins in yeast confirmed their capacity to transport glycerol. fpslDelta Yeast mutants expressing functional AnNIP1:1 and AnNIP1:2 showed increased glycerol uptake, and intra- and extracellular glycerol contents in agreement with their glycerol permease activity. Proper functional expression of AnNIP proteins in yeast needed the removal of the unique hydrophilic N-terminal domain of both proteins, which did not show to be necessary for their transport activities. (C) 2003 Elsevier Ireland Ltd. All rights reserved.