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      2. 黃單胞菌分泌蛋白的理化性質及特征分析
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        西南林業大學

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        中圖分類號:

        S435.1

        基金項目:

        國家自然科學基金項目(面上項目,重點項目,重大項目)


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

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          摘要:

          黃單胞菌(Xanthomonas campestris)屬于革蘭氏陰性細菌,主要危害十字花科蔬菜和核桃、杧果等經濟林,給農林作物造成了較大的經濟損失,嚴重危害著農林業產業的健康發展。分泌蛋白在植物病原真菌、細菌以及卵菌致病過程中發揮著重要的功能,尚未見有關黃單胞菌分泌蛋白理化性質及特征分析的報道。本研究以全基因組序列已經公布的黃單胞菌X. campestris B100、X. campestris pv.campestris str.8004、X. campestris CN14中分泌蛋白序列為基礎數據,采用Protscale、SMART、TargetP 2.0 Server等生物信息學分析軟件對上述分泌蛋白展開理化性質、保守結構域以及轉運肽等分析,結果表明,黃單胞菌中分泌蛋白理論等電點與氨基酸長度之間無明顯規律,平均44.73%的蛋白為不穩定蛋白,平均83.21%的蛋白總平均親水性小于0,屬于親水性蛋白,同時,分泌蛋白中平均有12個具有明顯的保守結構域,并且所有分泌蛋白定位于信號),轉運肽預測可能性分布也較為平均。該研究為深入解析黃單胞菌分泌蛋白的功能奠定堅實的理論基礎。

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