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机构地区:[1]周口师范学院生命科学与农学学院,周口466001
出 处:《分子植物育种》2017年第8期2937-2948,共12页Molecular Plant Breeding
基 金:河南省省科技厅攻关项目(152102110106);国家863计划项目(2012AA101105);河南省高等学校重点科研项目(16A210043)共同资助
摘 要:脱氢抗坏血酸还原酶(dehydroascorbate reductase,DHAR)能还原被氧化的抗坏血酸分子,是细胞中维持抗坏血酸氧化还原平衡状态的重要酶之一。为获得油菜DHAR蛋白家族成员的序列特征和功能差异信息,本研究基于GenBank油菜基因组数据库,执行TBLASTN比对分析,获得了油菜DHAR蛋白家族成员,并比较了序列特性、进化关系、亚细胞定位、基因结构与染色体定位,预测了其蛋白质互作和表达谱信息。结果表明,共获得了11个油菜DHAR蛋白质家族成员,分为2大类,第一类共5个成员,包括DHAR1和DHAR2,均定位于细胞质,除序列XP_013693221外,均由213或214个氨基酸残基组成,在进化关系、基因结构和互作蛋白质的种类和数量方面非常接近,可能具有比较接近的酶活性和功能;第二类共6个成员,均由DHAR3成员组成,定位于叶绿体中,除XP_013665393外,其余成员均由255个或257个氨基酸残基组成,与前两者进化关系较远,并且与其互作的蛋白质种类和数量也与前两者存在显著不同,可能与前两者的酶活性和功能有较大差异。本研究为揭示油菜DHARs的分子特征与功能差异性提供了一些新的见解。Dehydroascorbate reductase(DHAR), which can reduce oxidized ascorbic acid molecules, is one of the important reductases for maintaining an appropriate ascorbate redox state in cells. In order to obtain the sequence characteristics and functional differences of DHAR protein family members, In this study, we performed the TBLASTN comparison analysis and obtained the DHAR protein family members in Brassica napus L. based on the Gen Bank genome database, further we compared sequence characteristics, evolutionary relationships,subcellular localization, gene structure and chromosomal location, and predicted protein interactions and expression spectrum information. The results showed that a total of 11 members of DHAR protein family in Brassica napus L. were obtained, and could be divided into two categories, the first group consisted of five members, including DHAR1 and DHAR2, they were all localized in cytoplasm and composed of 213 or 214 amino acid residues, showed same performance in evolutionary relationships, gene structure and types and quantities of interacting proteins except for XP_013693221, so they may had a relatively close enzyme activity and function; the second group had six members, all consisted of DHAR3 members, they were all localized in chloroplast and composed of 255 or 257 amino acid residues except for XP_013665393, whose evolutionary relationship were far from the two formers, and types and quantities of interacting proteins were significantly different from the two formers, which indicated that they had great differences in enzymatic characteristics and function. This study provided some new insights for the molecular characteristics and functional divergence of DHARs in Brassica napus L..
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