期刊
MICROBIOLOGICAL RESEARCH
卷 166, 期 6, 页码 494-507出版社
ELSEVIER GMBH
DOI: 10.1016/j.micres.2010.10.002
关键词
Ornithine decarboxylase; Metarhizium anisopliae; Biocontrol
类别
资金
- Consejo Nacional de Ciencia y Tecnologia (CONACyT)
- Consejo Estatal de Ciencia y Tecnologia del Estado de Guanajuato (CONCyTEG)
- Secretaria de Educacion Publica (SEP)
- University of Guanajuato
- CONACyT, Mexico
- CONCyTEG, Mexico
The gene ODC1, which codes for the ornithine decarboxylase enzyme, was isolated from the entomopathogenic fungus, Metarhizium anisopliae. The deduced amino acid sequence predicted a protein of 447 amino acids with a molecular weight of 49.3 kDa that contained the canonical motifs of ornithine decarboxylases. The ODC1 cDNA sequence was expressed in Escherichia coli cells; radiometric enzyme assays showed that the purified recombinant protein had ornithine decarboxylase activity. The optimum pH of the purified Odd protein was 8.0-8.5, and the optimum reaction temperature was 37 degrees C. The apparent K-m for ornithine at a pyridoxal phosphate concentration of 20 mM was 22 mu M. The competitive inhibitor of ODC activity, 1,4-diamino-2-butanone (DAB), at 0.25 mM inhibited 95% of ODC activity. The ODC1 mRNA showed an increase at the beginning of appressorium formation in vitro. During the M. anisopliae invasion process into Plutella xylostella larvae, the ODC1 mRNA showed a discrete increase within the germinating spore and during appressorium formation. The second expression peak was higher and prolonged during the invasion and death of the insect. The ODC1 gene complements the polyamine auxotrophy of Yarrowia lipolytica odc null mutant. (C) 2010 Elsevier GmbH. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据