《植物生理学报》 2015, 51(1): 97-104
通信作者:王少敏;E-mail: sdipwsm@163.com;Tel: 0538-8298262
摘 要:
水孔蛋白(aquaporins, AQPs)是高效转运水分子的膜内在蛋白, 具有丰富的多样性, 在调控植物的水分关系中有重要作用。本研究采用Blast、ProtParam、SignalP和Swiss-Model等生物信息学软件, 对梨、苹果、黄瓜和番茄等22种植物AQP的理化性质、蛋白结构、系统发生树和功能域等进行了分析。结果表明, AQP蛋白氨基酸长度在284~295 aa之间, 理论等电点在7.67~9.30之间, 主要定位于质膜上, 除红叶藜外均为稳定性蛋白。二级结构由α螺旋、β折叠、无规则卷曲和延伸链等结构元件组成, 空间结构高度相似, 属于主要内在蛋白(MIP)家族。关键词:水孔蛋白; 理化性质; 系统进化; 结构特征
收稿:2014-09-12 修定:2014-12-22
资助:国家现代农业(梨)产业技术体系(CARS-29)。
Corresponding author: WANG Shao-Min; E-mail: sdipwsm@163.com; Tel: 0538-8298262
Abstract:
Aquaporins (AQPs), which are abundant in diversity, are the member of the major intrinsic proteins (MIPs) family with extraordinary ability to transport water, and play important roles in modulation of water relations in plants. In this study, the sequences characteristic, physical and chemical properties, protein structures, phylogenetic trees and functional domains of AQPs from Pyrus communis, Malus domestica, Cucumis sativus, Solanum lycopersicum, as well as other 18 plant species were analyzed and investigated using bioinformatics methods, such as Blast, ProtParam, SignalP and Swiss-Model. The results showed that the length of AQPs proteins were between 284–295 amino acids, and the isoelectric point was between 7.67–9.30. The AQPs proteins were mainly localized in the plasma membrane and belonged to stable proteins except Oxybasis rubra. The secondary structure of AQPs proteins were mainly composed of α-helix, β-turn, extended strand and random coil, and had highly similar spatial structures.Key words: aquaporins; physical and chemical properties; phylogenetic; structure characteristic
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