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Molecular cloning and sequence analysis of the chitinase gene from Bacillus thuringiensis serovar alesti

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Abstract

Endogenous chitinase plays a positive role in the pathogenicity of Bacillus thuringiensis to insect pests. The chitinase gene was cloned from B. thuringiensis serovar alesti strain HD-16, and the deduced 676 amino acid sequence showed a high degree of similarity with other Bacillus chitinases. Additionally, the deduced amino acid sequence showed that the protein contained an amino terminus signal peptide and consisted of a catalytic domain, a fibronectin type III domain and a chitin-binding domain. All three domains showed conserved sequences when compared to other bacterial chitinase or cellulase sequences.

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Authors and Affiliations

  1. Department of Bioengineering & Biotechnology, Huaqiao University, Fujian Quanzhou, 362011, P.R. China

    Yi Lin

  2. Key Lab of Pesticide Biochemistry, Ministry of Education, Fujian Agriculture and Forestry University, Fujian Fuzhou, 350002, P.R. China

    Guan Xiong

Authors
  1. Yi Lin
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  2. Guan Xiong
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Lin, Y., Xiong, G. Molecular cloning and sequence analysis of the chitinase gene from Bacillus thuringiensis serovar alesti . Biotechnology Letters 26, 635–639 (2004). https://doi.org/10.1023/B:BILE.0000023021.50213.ed

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  • DOI: https://doi.org/10.1023/B:BILE.0000023021.50213.ed

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