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真核生物中,SET蛋白在基因转录的表观遗传调控方面是必需的,基因转录通过催化组蛋白赖氨酸甲基化而受调控。某些病原性细菌和病毒可以分泌SET蛋白去修饰宿主基因组,进而抑制宿主细胞免疫反应。真菌中SET蛋白已有较为深入的研究。但是,分泌型SET蛋白的功能,很大程度上仍然未知。为了研究稻瘟病菌分泌型SET蛋白的功能,我们从稻瘟病菌数据库中搜索获得8个预测的分泌型SET蛋白,分别命名为MoSSP1-8。通过在线的生物信息学工具分析了Mo SSP蛋白功能结构域和理化特性。RNA-Seq数据揭示其中6个基因在侵染时期表达量上调。序列比对和进化分析结果表明,Mo SSP7及其真菌同源蛋白在SET结构域都具有保守的基序,并且在进化上关系较近。共聚焦显微观察结果表明,在侵染菌丝中MoSSP7蛋白主要集中在BIC上,这说明它是一个胞质效应因子。
In eukaryotes, the SET protein is essential for the epigenetic regulation of gene transcription, and gene transcription is regulated by the catalytic histone lysine methylation. Some pathogenic bacteria and viruses can secrete SET proteins to modify the host genome, thereby inhibiting the host cell immune response. SET proteins in fungi have been studied in more depth. However, the function of secretory SET proteins remains largely unknown. To study the function of the secreted SET protein of Magnaporthe grisea, we searched for eight predicted secretory SET proteins from the Magnaporthe grisea database and named them as MoSSP1-8. Mo SSP protein functional domains and physicochemical properties were analyzed by online bioinformatics tools. RNA-Seq data revealed that 6 of them were up-regulated during infection. Sequence alignment and phylogenetic analysis showed that both Mo SSP7 and their fungal homologs have conserved motifs in the SET domain and are closely related to evolution. Confocal microscopy results showed that the MoSSP7 protein was mainly concentrated on the BIC in the infected mycelium, indicating that it is a cytosolic factor.