• 中文核心期刊
  • CSCD来源期刊
  • 中国科技核心期刊
  • CA、CABI、ZR收录期刊

玉米大斑病菌热激蛋白Hsp70的鉴定和结构分析

Identification and Characterization of Heat Shock Protein Hsp70 in Setosphaeria turcica

  • 摘要:
      目的  对玉米大斑病菌Hsp70(Setosphaeria turcica Hsp70,StHsp70)基因家族进行结构鉴定和功能分析,为进一步阐明StHsp70在玉米大斑病菌生长发育和致病过程中的作用奠定基础。
      方法  利用玉米大斑病菌基因组数据库获得StHsp70基因家族成员,利用生物信息学方法进行理化性质、亚细胞定位、系统进化、保守基序和结构域分析,构建三级结构模型,并预测启动子等顺式作用元件。
      结果  StHsp70基因家族包括11个成员,分别为StHsp70-1~StHsp70-11,多数定位于细胞质,其次为内质网、线粒体和细胞核。系统进化分析结果表明,StHsp70家族成员可分为7类,其中Class A~F分别与酿酒酵母(Saccharomyces cerevisiae)热激蛋白SSA、SSB、SSC、KAR2、SSE、SSZ高度同源,而Class G在酵母中未发现其同源蛋白。结构预测分析发现,StHsp70家族成员都含有保守基序Motif 5,而Motif 6只存在于Class A~D中,Class G仅含有2~4种基序,与其他StHsp70家族成员存在显著差异。N端的NBD结构域类型在玉米大斑病菌和酵母不同Hsp70类型间存在显著差异,可能与亚细胞定位有关。不同类型StHsp70的C末端结构和延伸性变化较大,特别是Class G的StHsp70与其他类型具有显著区别,可能与底物的多样性有关。
      结论  玉米大斑病菌Hsp70家族11个成员可以分为7类,其中Class G的4个成员在理化性质和结构特征上都与其他成员具有显著的区别,表明StHsp70属于多功能分子伴侣家族。

     

    Abstract:
      Objective  Identification and characteristics of Hsp70 family in Setosphaeria turcica were studied to facilitate elucidating their roles in the growth, development, and pathogenicity of the microbe.
      Methods  Members of StHsp70 family were identified from the S. turcica genome database. Physicochemical properties, subcellular localization, phylogenetic evolution, conserved motifs, and domains of the genes analyzed by bioinformatics methods.
      Results  Eleven members, StHsp70-1 to StHsp70-11, were identified from the database. Most of them were predicated to locate in the cytoplasmic as well as in endoplasmic reticulum, mitochondrial, and nucleus in lesser amounts. The phylogenetic analysis divided the members into 7 categories including Classes A−F that showed a high homology with the heat shock proteins SSA, SSB, SSC, KAR2, SSE, and SSZ of Saccharomyces cerevisiae, respectively, and Class G that had none with what were found in yeasts. All StHsp70s contained conserved motif 5, but motif 6 existed in Class A−D only. Class G had only motifs 2−4 making the class significantly different from the others. The variations in subcellular localization might be the reason of the significant N-terminal differences in the NBD domains of the Hsp70 classes of S. turcica from those of yeast. Whereas the considerably varied C-terminal structure and extensibility among the classes, especially on the StHsp70s of Class G, might contribute to the diversity of substrates.
      Conclusion  The 11 members of Hsp70 family of S. turcica could be divided into 7 classes with 4 members in Class G being significantly different from the others in physicochemical properties and structure. It indicated that the genes were of multifunctional molecular chaperones.

     

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