International Journal of Industrial Entomology and Biomaterials

Korean Society of Sericultural Science (한국잠사학회)
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cDNA Sequence and mRNA Expression of a Putative Alcohol Dehydrogenase from the Mole Cricket, Gryllotalpa orientalis

  • Kim, Iksoo (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technology) ;
  • Lee, Kwang-Sik (College of Natural Resources and Life Science, Dong-A University) ;
  • Jin, Byung-Rae (College of Natural Resources and Life Science, Dong-A University) ;
  • Lee, Young-Sin (Department of Life Science, Hoseo University, Asan City) ;
  • Ryu, Kang-Sun (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technology)
  • Published : 2003.09.01
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Abstract

Alcohol dehydrogenases (AHDs) are enzymes responsible for the catalysis of the reversible conversion of various alcohols to their corresponding aldehydes and ketonesis. Until now cDNA sequences of ADH gene is informed exclusively from several diptean species. We describe here the cDNA sequence and mRNA expression of a putative ADH gene from the mole cricket, Gryllotalpa orientalis, and phylogenetic relationships among known insect ADHs. The G. orientalis ADH cDNA sequences comprised of 798 bp encoding 266 amino acid residues. The multiple sequence alignment of G. orientalis ADH gene and known dipteran ADHs shared 100％ identity in the nine amino acid residues that are important for the enzymatic activity in Drosophila melanogaster. Percent sequence identity ranged from 25％ to 32％ among all insect ADHs including both types of ADHs. G. orientalis ADH gene showed no clear resemblance to any dipteran species and type. Phylogenetic analysis of the deduced amino acid sequences of G. orientalis ADH gene with available dipteran ADH genes including both types of ADHs further confirmed that the G. orientalis ADH gene is not clearly assigned to either type of ADHs. Northern blot analysis revealed a stronger signal in the fat body than midgut and epidermis, indicating that the fat body possibly is a main site for the synthesis of the G. orientalis ADH protein.

Keywords

References

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