Geng Z.,Laboratory for Conservation and Utilization of Bio resources |
Geng Z.,Yunnan University |
Zhu W.,Laboratory for Conservation and Utilization of Bio resources |
Zhu W.,Yunnan University |
And 8 more authors.
Biotechnology Advances | Year: 2014
The ascomycete fungus, Fusarium graminearum (teleomorph Gibberella zeae), is the most common causal agent of Fusarium head blight (FHB), a devastating disease for cereal crops worldwide. F. graminearum produces ascospores (sexual spores) and conidia (asexual spores), which can serve as disease inocula of FHB. Meanwhile, Fusarium-infected grains are often contaminated with mycotoxins such as trichothecenes (TRIs), fumonisins, and zearalenones, among which TRIs are related to the pathogenicity of F. graminearum, and these toxins are hazardous to humans and livestock. In recent years, with the complete genome sequencing of F. graminearum, an increasing number of functional genes involved in the production of secondary metabolites, hyphal differentiation, sexual and asexual reproduction, virulence and pathogenicity have been identified from F. graminearum. In this review, the secondary metabolite synthesis, hyphal development and pathogenicity related genes in F. graminearum were thoroughly summarized, and the genes associated with secondary metabolites, sexual reproduction, energy metabolism, and pathogenicity were highlighted. © 2013 Elsevier Inc.
Mi Q.,Laboratory for Conservation and Utilization of Bio resources |
Yang J.,Laboratory for Conservation and Utilization of Bio resources |
Ye F.,Laboratory for Conservation and Utilization of Bio resources |
Gan Z.,Laboratory for Conservation and Utilization of Bio resources |
And 4 more authors.
Process Biochemistry | Year: 2010
The fungus Pochonia chlamydosporia is a biocontrol agent with commercial potential for root-knot and cyst nematodes. In this study, a gene (designated pcchi44) encoding an extracellular endochitinase was isolated for the first time from P. chlamydosporia using degenerate primers and a genome walking technique. The 2385-bp pcchi44 sequence is interrupted by three introns and encodes a 424-amino acid polypeptide. The cDNA sequence of pcchi44 was amplified via reverse transcription polymerase chain reaction and overexpressed in Escherichia coli BL21. The recombinant chitinase PCCHI44 was purified as a protein of ca. 44 kDa with an optimal activity at pH 6.0 and 50 °C. The Vmax and Km value of PCCHI44 using 4-methylumbelliferyl-β-d-N,N′,N″-triacetylchitotrioside as substrate were 8.37 × 10-3 μM s-1 and 9.65 μM, respectively. The hydrolytic activity of PCCHI44 could be completely inhibited by acetazolamide. The chitinase PCCHI44 could damage eggs of both the root-knot nematode Meloidogyne incognita and the insect Bombyx mori. © 2010 Elsevier Ltd. All rights reserved.