| 刺槐Na+/H+逆向转运蛋白RpNHX1基因的分离和生物信息学分析 |
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| 引用本文： | 于学宁,刘欣玲,董秀春,樊金会,曹帮华.刺槐Na+/H+逆向转运蛋白RpNHX1基因的分离和生物信息学分析[J].分子植物育种,2007,5(6):775-784. |
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| 作者姓名： | 于学宁 刘欣玲 董秀春 樊金会 曹帮华 |
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| 作者单位： | 1. 山东农业大学林学院,泰安,271018
2. 山东艺术学院校园管理中心,济南,250307 |
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| 摘 要： | 盐分胁迫严重影响植物生长和产量.为了研究木本植物对盐分的适应性,利用5'RACE技术,从刺槐中克隆得到液泡Na /H 逆向转运蛋白基因RpNHX1.该基因长度为2 281 bp,含有一个开放阅读框,编码535氨基酸残基组成的蛋白,该蛋白序列与大豆GmNHX1和拟南芥AtNHX1相似,氨基酸的同源性分别达85%和69%,RpNHX1属于NHX亚族的NHX-I分枝.用生物信息学的方法预测RpNHX1具有所有Na /H 逆向转运蛋白共同的结构特点,即含有疏水的N末端,10个跨膜螺旋区域和一个具有调节功能的C端亲水区域,其中氨氯吡嗪咪敏感基序和CaM结合域也是保守的.在4和5的螺旋区域之间,存在有一串带负电荷氨基酸,显示出有规律的排列模式,这些模式在生物界中的Na /H 转运蛋白中是保守的.结合亲疏水资料,我们认为Na /H 转运通道结构可能存在于这一区域.另外,也分析了RpNHX1可能的糖基化、酰基化和磷酸化位点.从这些数据中可以看出,RpNHX1可能在细胞中起到Na 区隔化作用.
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| 关 键 词： | Na /H 逆向转运蛋白基因 盐胁迫 生物信息学分析 刺槐 Na /H antiporter gene Salt tolerance Bioinformational analysis Robina pseudoacacia L. |
Isolation and Bioinformational Analysis of Na+/H+ Antiporter RpNHX1 Gene from Black Locust |
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| Yu Xuening,Liu Xinling,Dong Xiuchun,Fan Jinhui,Cao Banghua.Isolation and Bioinformational Analysis of Na+/H+ Antiporter RpNHX1 Gene from Black Locust[J].Molecular Plant Breeding,2007,5(6):775-784. |
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| Authors: | Yu Xuening Liu Xinling Dong Xiuchun Fan Jinhui Cao Banghua |
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| Institution: | 1. College of Forestry, Shandong Agricultural University, Taian, 271018; 2. Campus Administration Center, Shandong Art College, Jinan, 250307 |
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| Abstract: | Salinity stress impacts severely plant growth and yield. In order to study wood plant salt adaptability, a vacuolar Na+/H+antiporter RpNHX1 gene was cloned from Robinia pseudlacacia L. by 5' RACE strategy. The gene is 2 281 bp in length, withan open reading frame encoding a 535 amino acid protein, which is close similar to Glycine max GmNHX1 and Arabidopsis AtNHX1 by 85% and 69% identity respectively, and belongs to NHX-I cluster in NHX subfamily. Bioinformation predicts that RpNHX1 has a common structure in all of Na+/H+ antiporters, which composed of a hydrophobic N terminus, 10 transmembrane helix region and a regulatory hydrophilic C region, in which an amiloride-sensitive motif and a CaM binding domain are conserved. A tandem of negatively charged amino acid between helix 4 and 5 shows regularly arranged patterns, conservatively presenting in Na+/H+ transporters among organisms, where a Na+/H+transport pore structure was proposed combined with its hydropathy profile. Additionally, the glycosylation, N-myristoylation and phosphorylation sites were also examined. From these data, it is thought that RpNHX1 may be competent for Na+compartmentation in cells. |
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| Keywords: | Na /H antiporter gene Salt tolerance Bioinformational analysis Robina pseudoacacia L |
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