Analysis of Secretary Proteins in the Genome of the Plant Pathogenic Fungus Botrytis Cinerea

The signal peptides prediction algorithm SignalP v3.0, subcellular protein location prediction algorithm TargetP.v1.1, potential GPI-anchor sites prediction algorithm big-PI predictor, trans-membrane domains prediction algorithm TMHMM v2.0 and bioinformatics algorithm MEME were used to analyze 16446 protein sequences of Botrytis cinerea. The results showed that there were 579 deduced secretary proteins. Among these proteins, the minimum and maximum of open read frame were 102 bp and 4848 bps respectively and mean score was 1271 bps. The signal peptides' length was concentrated to 16 similar to 39 amino acids and the average length was 21. 122 of these proteins contain the highly conserved host-targeting-motif RxLx within 100 residues adjacent to the signal peptide cleavage site. According to PEDNAT and COG of GenBank database, this motif's functions include metabolism modification and cell secretion etc. We blast those putative secretary proteins with RxLx motif in GenBenk and found 47.54% of them have highly conserved homologues in other species, among them 74.1% have putative protein domains. This means these proteins may be more stable or earlier origin. We suppose these proteins are candidate participating in the pathogenesis of Botrytis cinerea but we still need more experimental evidence to confirm their definite functions.