Trypsin-like proteins of the fungi as possible markers of pathogenicity.
Sequences of peptidases with conserved motifs around the active site residues that are characteristic of trypsins (similar to trypsin peptidases, STP) were obtained from publicly-available fungal genomes and related databases. Among the 75 fungal genomes, 29 species of parasitic Ascomycota contained genes encoding STP and their homologs. Searches of non-redundant protein sequences, patented protein sequences, and expressed sequence tags resulted in another 18 STP sequences in 10 fungal species from Ascomycota, Basidiomycota, and Zygomycota. A comparison of fungi species containing STP sequences revealed that almost all are pathogens of plants, animals or fungi. A comparison of the primary structure of homologous proteins, including the residues responsible for substrate binding and specificity of the enzyme, revealed three groups of homologous sequences, all presumably from S1 family: trypsin-like peptidases, chymotrypsin-like peptidases and serine peptidases with unknown substrate specificity. Homologs that are presumably functionally inactive were predicted in all groups. The results in general support the hypothesis that the expression of trypsin-like peptidases in fungi represents a marker of fungal phytopathogenicity. A phylogenetic tree was constructed using peptidase and homolog amino acid sequences, demonstrating that all have noticeable differences and almost immediately deviate from the common root. Therefore, we conclude that the changes that occurred in STP of pathogenic fungi in the course of evolution represent specific adaptations to proteins of their respective hosts, and mutations in peptidase genes are important components of life-style changes and taxonomic divergence.
Faculty of Bioengineering and Bioinformatics, Moscow State University, Moscow 119991, Russia.
Aleksej G
AG
Dubovenko
Yakov E
YE
Dunaevsky
Mikhail A
MA
Belozersky
Brenda
B
Oppert
Jeffrey C
JC
Lord
Elena N
EN
Elpidina
D020816:Amino Acid Motifs; D000818:Animals; D001203:Ascomycota / Q000145:classification / Q000201:enzymology / Q000235:genetics / Q000472:pathogenicity; D001487:Basidiomycota / Q000145:classification / Q000201:enzymology / Q000235:genetics / Q000472:pathogenicity; D019295:Computational Biology / Q000379:methods; D005656:Fungal Proteins / Q000235:genetics* / Q000378:metabolism; D005658:Fungi / Q000145:classification / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity*; D016681:Genome, Fungal / Q000235:genetics; D006801:Humans; D009181:Mycoses / Q000382:microbiology*; D010447:Peptide Hydrolases / Q000235:genetics / Q000378:metabolism; D010802:Phylogeny; D010935:Plant Diseases / Q000382:microbiology*; D016415:Sequence Alignment; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D014357:Trypsin / Q000235:genetics* / Q000378:metabolism
D005656:Fungal Proteins; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; D014357:Trypsin