| 盐生杜氏藻D.salina和D.bardwil苹果酸脱氢酶基因的克隆和序列分析 |
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| 引用本文： | 贺庆华,郑玉才,林亚秋,聂玲玲.盐生杜氏藻D.salina和D.bardwil苹果酸脱氢酶基因的克隆和序列分析[J].安徽农业科学,2008,36(11):4435-4437. |
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| 作者姓名： | 贺庆华 郑玉才 林亚秋 聂玲玲 |
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| 作者单位： | 西南民族大学生命科学与技术学院,四川成都,610041;西南民族大学生命科学与技术学院,四川成都,610041;西南民族大学生命科学与技术学院,四川成都,610041;西南民族大学生命科学与技术学院,四川成都,610041 |
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| 基金项目： | 西南民族大学资助课题;国家民委资助课题. |
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| 摘 要： | 目的]探讨利用盐生杜氏藻的MDH基因提高农作物耐盐性能的可行性。方法]对盐生杜氏藻2个种(D.salina和D.bardwil)的苹果酸脱氢酶(MDH)进行克隆,并对它们的序列进行比较分析。结果]盐生杜氏藻2个藻种MDH基因的全编码区序列分别长1 303 bp和1 288 bp,分别编码434和429个氨基酸的2个蛋白,经过亚细胞定位预测和相似性搜索,认为这两个蛋白应定位于叶绿体,即属于叶绿体型苹果酸脱氢酶。两个藻种的MDH基因编码区的核酸序列相似性为88.6%,氨基酸序列的相似性为93.5%,去除预测的信号肽序列后两者氨基酸的相似性达到97.4%。经过分子建模分析发现,D.salina的MDH相对于D.bardwil的MDH,大部分的氨基酸突变都位于蛋白分子表面,而且大多数位于分子表面的突变都是非极性氨基酸和极性氨基酸之间的转变。结论]推测这些蛋白分子表面氨基酸残基的突变可能是D.salina的MDH对高盐浓度环境的适应结果。
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| 关 键 词： | 苹果酸脱氢酶 盐生杜氏藻 克隆 分子建模 |
| 文章编号： | 0517-6611(2008)11-04435-02 |
| 修稿时间： | 2008年2月1日 |
Cloning and Sequence Analysis of Malic Dehydrogenase Genes from Dunaliella D.salina and D.bardwil |
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| HE Qing-hua.Cloning and Sequence Analysis of Malic Dehydrogenase Genes from Dunaliella D.salina and D.bardwil[J].Journal of Anhui Agricultural Sciences,2008,36(11):4435-4437. |
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| Authors: | HE Qing-hua |
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| Abstract: | Objective] The research aimed to discuss the feasibility of increasing the tolerance of crops to salt by using malic dehydrogenase(MDH) gene in Dunaliella.Method] The MDH from 2 varieties of Dunaliella(D.salina and D.bardwil) was cloned and their sequences were compared.Result] The sequence in the whole coding region of MDH gene in 2 varieties of Dunaliella were 1 303 and 1 288 bp,which encoded 2 proteins with 434 and 429 amino acids.Through subcellular targeting prediction and similarity searching,it was thought that these two proteins should be located in chloroplast,i.e.they belonged to chloroplast MDH.In the coding region of MDH gene between 2 varieties of Dunaliella,the similarity of nucleotides sequence was 88.6% and that of amino acids sequence was 93.5%.After the predicted signal peptide sequences were removed,the amino acid similarity between the two reached 97.4%.Through molecular modeling analysis,it was found that compared with MDH of D.bardwil,most mutations of amino acids lied on the molecular surface of protein in MHD of D.salina.Most mutations on the molecular surface were transformed between non-polar amino acids and polar amino acids.Conclusion] It can be predicted that the mutations of amino acid residues on the molecular surface of protein might be a adaptation consequence of MDH in D.salina to the environment with high-concn.salt. |
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| Keywords: | Malic dehydrogenase Dunaliella Cloning Molecular modeling |
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