部分模式真菌中Prp5蛋白生物信息学分析

【目的】利用生物信息学方法对7种模式真菌中Prp5蛋白进行分析，为进一步研究Prp5蛋白在RNA剪接中的作用及其他独特的生物学功能提供基础。【方法】利用多种在线网站与软件分析和预测了稻瘟菌、裂殖酵母、酿酒酵母、粗糙脉胞菌、构巢曲霉、新生隐球菌、白色念珠菌Prp5蛋白的基本特性、二级结构、结构域及三级结构，同时对7种Prp5蛋白进行同源比对，并构建了系统进化树。【结果】所有研究蛋白均为不稳定的亲水性蛋白，稻瘟菌、粗糙脉胞菌、构巢曲霉的Prp5蛋白及裂殖酵母Prp11蛋白均呈碱性，而新生隐球菌与白色念珠菌的Prp5蛋白显酸性；进化分析显示稻瘟菌和粗糙脉胞菌亲缘关系最近，且7种模式生物被分为两个类群；二级结构以α螺旋为主；所有蛋白均含有DEAD和Helicase_C功能结构域；三级结构分析显示DEAD结构域较稳定，而Helicase_C结构域在空间结构上存在一定的变化。【结论】Prp5蛋白在不同真菌中具有保守性，因此可能发挥相似的生物学功能。然而酿酒酵母Prp5蛋白结构上略有变化，表明其在功能上可能具有一定独特性。研究结果对指导Prp5蛋白的进一步研究具有一定的参考价值。

The bioinformatics analysis of Prp5 proteins in some model fungi

Objective] Prp5 proteins were analyzed by bioinformatics in seven model fungi. The purpose is to lay a foundation for further experimental study of Prp5 in RNA splicing and other unique biological function. Methods] Some basic characteristics, secondary structure, domain and tertiary structure were analyzed and predicted using online webs and softwares in Magnaporthe oryzae, Schizosaccharomyces pombe, Saccharomyces cerevisiae, Neurospora crassa, Aspergillus nidulas, Cryptococcus neoformans and Candida albicans. Meanwhile, the homologies of Prp5 proteins of seven species were compared, based on which a phylogenetic tree was plotted. Results] The results showed that all studied proteins are unstable hydrophilic protein. Prp5 in Magnaporthe oryzae, Neurospora crassa, Aspergillus nidulas and Prp11 in Schizosaccharomyces pombe were alkaline proteins whereas Prp5 proteins in Cryptococcus neoformans and Candida albicans were acidic. Evolution analysis showed that the seven model fungi are divided into two groups and Magnaporthe oryzae and Neurospora crassa have the closest genetic relationship. Alpha helix is based structure. All proteins contain DEAD and Helicase_C domain. Tertiary structure analysis showed that DEAD domain is stable, while domain Helicase_C showed some changes on the spatial structure. Conclusion] Prp5 protein may play similar role on account of their conservative structure in different fungi. However, Prp5 protein in Saccharomyces cerevisiae is a little different on spatial structure, suggesting that it may have some unique functions. These results will provide guidance for further study about Prp5 in the experiments.