北方农业学报 ›› 2020, Vol. 48 ›› Issue (3): 39-46.doi: 10.12190/j.issn.2096-1197.2020.03.06

• 种质资源·分子生物学 • 上一篇    下一篇

9种真菌中分支点结合蛋白的生物信息学分析

邱凯华, 李晓驹, 方淑梅, 梁喜龙   

  1. 黑龙江八一农垦大学,黑龙江 大庆 163319
  • 收稿日期:2020-03-18 出版日期:2020-06-20 发布日期:2020-08-14
  • 通讯作者: 梁喜龙(1976—),男,教授,博士,硕士生导师,主要从事作物化学调控与抗逆生理等方面的研究工作。
  • 作者简介:邱凯华(1994—),女,硕士研究生,研究方向为寒地作物生长控制原理与技术。
  • 基金资助:
    黑龙江省自然科学基金项目(C2016047); 黑龙江省科技厅指导项目(GZ13B014); 黑龙江八一农垦大学研究生创新科研项目(YJSCX2019-Y14)

Bioinformatic analysis of branchpoint-bridging protein in nine fungi

QIU Kaihua, LI Xiaoju, FANG Shumei, LIANG Xilong   

  1. Heilongjiang Bayi Agricultural University,Daqing 163319,China
  • Received:2020-03-18 Online:2020-06-20 Published:2020-08-14

摘要: 【目的】进一步了解分支点结合蛋白(branchpoint-bridging protein,BBP)在真菌中的生物学功能。【方法】利用多种生物信息学软件和网站对9种真菌[稻瘟病菌(Pyricularia oryzae)、酿酒酵母(Saccharomyces cerevisiae)、小麦全蚀病菌(Gaeumannomyces tritici)、粗糙脉孢菌(Neurospora crassa)、西瓜炭疽病菌(Colletotrichum orbiculare)、白僵菌(Beauveria bassiana)、尖孢镰刀菌(Fusarium oxysporum)、水稻恶苗病菌(Fusarium fujikuroi)和立枯丝核菌(Rhizoctonia solani)]的BBP进行预测分析,包括蛋白与基因的基本信息、理化性质、亚细胞定位、信号肽与跨膜螺旋结构、蛋白质空间构象及磷酸化位点与SUMO化位点,并构建系统进化树。【结果】BBP的分子量在50 812.65~68 306.99 Da,均为碱性不稳定的亲水性蛋白,存在于细胞核中,无信号肽及跨膜螺旋,磷酸化位点及占比相似,α螺旋是主要的二级结构,均具有SF1-HH、KH_dom和Znf_CCHC结构域,然而酿酒酵母ONH80283.1和立枯丝核菌CCO28600.1与其他真菌BBP相比在分子进化和空间构象上有较明显差异,且CCO28600.1的SUMO化位点较多。【结论】9种常见真菌中,酿酒酵母和立枯丝核菌的BBP结构比较特殊,BBP在稻瘟病菌、小麦全蚀病菌、粗糙脉孢菌、西瓜炭疽病菌、白僵菌、尖孢镰刀菌、水稻恶苗病菌中进化比较保守。

关键词: 分支点结合蛋白, 真菌, 生物信息学分析, SUMO化

Abstract: 【Objective】To further analysis of the biological functions of branchpoint-bridging protein (BBP) in fungi.【Methods】A variety of bioinformatics software and websites are used to predict and analyze the BBP in nine fungi (Pyricularia oryzaeSaccharomyces cerevisiaeGaeumannomyces triticiNeurospora crassaColletotrichum orbiculareBeauveria bassianaFusarium oxysporumFusarium fujikuroi and Rhizoctonia solani),including the basic information of the protein and gene,the physical and chemical properties,the subcellular localization and signal peptide and protein conformation and transmembrane helical structure,phosphorylation site on a SUMO loci,and build the system of the evolutionary tree.【Results】The molecular weight of BBP range from 50 812.65 Da to 68 306.99 Da.They were all unstable hydrophilic proteins located in the nucleus.There were no signal peptides and transmembrane helixes.Alpha helix was the main secondary structure and SF1-HH,KH_dom and Znf_CCHC domains exist in all BBPs of the nine fungi.However,ONH80283.1 of Saccharomyces cerevisiae and CCO28600.1 of Rhizoctonia solani showed different molecular evolution and spatial conformation to BBPs of other fungi.The phosphorylation types and percentages of BBPs were similar in the nine fungi,but CCO28600.1 had more SUMO sites.【Conclusion】Among the nine common fungi,the BBP structure of Saccharomyces cerevisiae and Rhizoctonia solani was relatively special,and the evolution of BBP was relatively conservative in Pyricularia oryzae,Gaeumannomyces tritici,Neurospora crassa,Colletotrichum orbiculare,Beauveria bassiana,Fusarium oxysporum and Fusarium fujikuroi.

Key words: Branchpoint-bridging protein, Fungi, Bioinformatics analysis, SUMO

中图分类号: 

  • Q949.32