立枯丝核菌AG-3全基因组分泌蛋白的预测分析

Prediction and analysis of the secreted proteins from the genome of Rhizoctonia solani AG-3

[目的]预测、分析立枯丝核菌AG-3全基因组范围内的分泌蛋白,并明确其基本特征,筛选其效应蛋白。[方法]依据已经公布的立枯丝核菌AG-3全基因组数据库中的12 726个蛋白序列,利用信号肽预测软件SignalP-4.1,细胞器定位分析软件ProtComp 9.0,跨膜螺旋结构预测软件TMHMM 2.0,GPI-锚定位点预测软件big-PI Fungal Predictor和亚细胞器中蛋白定位分布预测软件TargetP-1.1进行典型分泌蛋白的预测分析,并用LipoP-1.0进行信号肽切割位点的预测分析,最后对预测得到的分泌蛋白通过EffectorP进行效应蛋白的预测。[结果]在立枯丝核菌AG-3中有401个蛋白被预测为分泌蛋白,其编码蛋白长度集中于100~600 aa。信号肽长度介于11~35 aa之间,-3至-1位置上的氨基酸相对保守,切割位点为A-X-A类型,可被SpⅠ型信号肽酶识别并切割。在预测得到的分泌蛋白中通过EffectorP筛选得到140个效应蛋白。[结论]通过全基因组预测得到401个具有典型分泌蛋白特征的蛋白,从预测的分泌蛋白中筛选得到140个效应蛋白。

[Objective] To predict and analyze the genome-wide secreted proteins of Rhizoctonia solani AG-3,and to clarify their basic characteristics and screen their effector proteins.[Method] Based on the published 12 726 protein sequences in the whole genome database of R.solani AG-3,we used SignalP-4.1 signal peptide prediction software,ProtComp 9.0 organelle localization analysis software,TMHMM 2.0 transmembrane helix structure prediction software,GPI-anchor localization site prediction software big-PI Fungal Predictor and TargetP-1.1 for predicting protein localization distribution in subcellular organelles,and LipoP-1.0 for predicting signal peptide cleavage sites,and finally EffectorP for predicting effector proteins for the obtained secreted proteins.[Result] There were 401 proteins predicted as secretory proteins in R.solani AG-3,and their coding protein lengths were concentrated in the range of 100-600 aa.The signal peptide lengths ranged from 11 to 35 aa,and the amino acids at the-3 to-1 positions were relatively conserved,and the cleavage sites were of type A-X-A,which could be recognized and cleaved by Sp type Ⅰ signal peptidase.Among the predicted secreted proteins obtained,140 effector proteins were obtained by EffectorP screening.[Conclusion]401 proteins with typical secretory protein characteristics were obtained by genome-wide prediction,and 140 effector proteins were obtained from the predicted secretory proteins by screening.