Expression of Aquaporin BnPIP-like Gene from Rapeseed (Brassica napus) Enhances Salt Resistance in Yeast (Pichia pastoris)

文献类型： 外文期刊

第一作者： Li, Hao-Jie

作者： Li, Hao-Jie;Zhang, Jin-Fang;Cui, Cheng;Jiang, Jun;Zheng, Ben-Chuan;Jiang, Liang-Cai;Tan, Hao;Zhang, Bi

作者机构：

关键词： Brassica napus;Aquaporin;Salt resistance;Eukaryotic expression

期刊名称：INTERNATIONAL JOURNAL OF AGRICULTURE AND BIOLOGY （ 影响因子：0.822； 五年影响因子：0.906 ）

ISSN： 1560-8530

年卷期： 2016 年 18 卷 6 期

页码：

收录情况： SCI

摘要： A new aquaporin (AQP) BnPIP-like gene was isolated and sequenced from rapeseed (Brassica napus L.). It encoded a putative protein with 281 amino acids, sharing 95.3% identity with Arabidopsis plasma membrane intrinsic proteins (PIP, Genbank: NP_195236.1). Prediction of transmembrane structure showed that BnPIP-like gene contained five loops and six transmembrane helices. Online analysis also indicate that BnPIP-like protein existed as homo-tetramers. In order to research its functions in eucaryon, BnPIP-like gene was fused into the pPIC3.5K and then the recombinant vector, as well as the pPIC3.5K, were induced into methylotrophic yeast (Pichia pastoris Strain GS115), respectively. In BMMY media, the BnPIP-like protein was sufficiently expressed after methanol (MeOH) induction for 24 h. The salt stress (300 mM NaCl) treatment was operated after 18 h of normal growth conditions. The OD600 values of BnPIP-like-transgenic P. pastoris and the control were determined every 12 h. The growth curves were obtained and it showed that the growth of both P. pastoris with or without BnPIP-like protein was obviously inhibited. However, the concentrations of BnPIP-like-transgenic P. pastoris was always higher than the control, indicating that the inhibition of growth in BnPIP-like-transgenic P. pastoris was slighter because of the over-expression of BnPIP-like gene. Thus the resistance to salt explained the eukaryotic functions of BnPIP-like protein. Moreover, it provided a theoretical possibility for a more comprehensively industrial utilization of fermenting yeast. (C) 2016 Friends Science Publishers

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