黄单胞菌分泌蛋白的理化性质及特征分析
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西南林业大学

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S435.1

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国家自然科学基金项目(面上项目,重点项目,重大项目)


Analysis of Physicochemical Properties and Characteristics of Xanthomonas campestris Secretary Protein
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Southwest Forestry University

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    摘要:

    黄单胞菌(Xanthomonas campestris)属于革兰氏阴性细菌,主要危害十字花科蔬菜和核桃、杧果等经济林,给农林作物造成了较大的经济损失,严重危害着农林业产业的健康发展。分泌蛋白在植物病原真菌、细菌以及卵菌致病过程中发挥着重要的功能,尚未见有关黄单胞菌分泌蛋白理化性质及特征分析的报道。本研究以全基因组序列已经公布的黄单胞菌X. campestris B100、X. campestris pv.campestris str.8004、X. campestris CN14中分泌蛋白序列为基础数据,采用Protscale、SMART、TargetP 2.0 Server等生物信息学分析软件对上述分泌蛋白展开理化性质、保守结构域以及转运肽等分析,结果表明,黄单胞菌中分泌蛋白理论等电点与氨基酸长度之间无明显规律,平均44.73%的蛋白为不稳定蛋白,平均83.21%的蛋白总平均亲水性小于0,属于亲水性蛋白,同时,分泌蛋白中平均有12个具有明显的保守结构域,并且所有分泌蛋白定位于信号),转运肽预测可能性分布也较为平均。该研究为深入解析黄单胞菌分泌蛋白的功能奠定坚实的理论基础。

    Abstract:

    Xanthomonas campestris belong to Gram-negative bacteria, which mainly harm cruciferous vegetables and economic forests such as walnuts and mangosteens, causing great economic losses to agricultural and forestry crops and seriously harming the healthy development of the agricultural and forestry industry. Secreted proteins play an important role in the pathogenic process of plant pathogenic fungi, bacteria, and oomycetes. There have been no reports on the physical and chemical properties and characteristics of secreted proteins of Xanthomonas. This study uses the secreted protein sequences of X. campestris B100, X. campestris pv. campestris str.8004, and X. campestris CN14 with the published genome-wide sequence as the basic data, and uses Protscale, SMART, TargetP 2.0 Server, and other organisms. Informatics analysis software analyzes the physicochemical properties, conserved domains, and transit peptides of the above-secreted proteins. The results show that there are no obvious rule between the theoretical isoelectric point of secreted proteins in X. campestris and the length of amino acids. The average 44.73% of the protein is Unstable protein, with an average of 83.21% of the total protein, the average hydrophilicity is less than 0, which is a hydrophilic protein. At the same time, 12 of the secreted proteins of each X. campestris have an obvious conserved domain, and all secreted The protein is localized at S (signal peptide), and the predicted probability distribution of the transit peptide is also relatively even. This study lays a solid theoretical foundation for the in-depth analysis of the function of X. campestris secreted proteins.

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  • 收稿日期:2020-06-15
  • 最后修改日期:2020-07-08
  • 录用日期:2020-09-17
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