Characterization of an extracellular serine protease gene from the nematophagous fungus Lecanicillium psalliotae.
The gene encoding a cuticle-degrading serine protease was cloned from three isolates of Lecanicillium psalliotae (syn. Verticillium psalliotae) by 3' and 5' RACE (rapid amplification of cDNA ends) method. The gene encodes for 382 amino acids and the protein shares conserved motifs with subtilisin N and peptidase S8. Comparison of translated cDNA sequences of three isolates revealed one amino acid polymorphism at position 230. The deduced protease sequence shared high degree of similarities to other cuticle-degrading proteases from other nematophagous fungi.
Yang
Jinkui
J
Laboratory for Conservation and Utilization of Bio-resources, Yunnan University, 650091, Kunming, PR China. kqzhang111@yahoo.com.cn
Huang
Xiaowei
X
Tian
Baoyu
B
Sun
Hui
H
Duan
Junxin
J
Wu
Wenping
W
Zhang
Keqin
K
D020816:Amino Acid Motifs; D001203:Ascomycota / Q000201:enzymology / Q000235:genetics*; D003001:Cloning, Molecular; D005656:Fungal Proteins / Q000235:genetics*; D005800:Genes, Fungal; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics*
D005656:Fungal Proteins; D012697:Serine Endopeptidases