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 sub...

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Bibliographic Details
Published in:Biotechnology letters 2005-09, Vol.27 (17), p.1329-1334
Main Authors: Yang, Jinkui, Huang, Xiaowei, Tian, Baoyu, Sun, Hui, Duan, Junxin, Wu, Wenping, Zhang, Keqin
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino acids
Ascomycota - enzymology
Ascomycota - genetics
Biological and medical sciences
Biotechnology
Cloning, Molecular
Fundamental and applied biological sciences. Psychology
Fungal Proteins - genetics
Genes, Fungal
Lecanicillium psalliotae
Molecular Sequence Data
Proteins
Sequence Homology, Amino Acid
Serine Endopeptidases - genetics
Verticillium
Verticillium psalliotae
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Summary: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.
ISSN:0141-5492
1573-6776
DOI:10.1007/s10529-005-0482-1