Molecular cloning of chitinase cDNAs from the silkworm, Bombyx mori and the fall webworm, Hyphantria cunea

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cDNAs encoding chitinases were cloned and characterized fr om Bombyx mori and Hyphantria cunea. and their gene expression during the metamorphosis was also studied. The chitinase cDNA from B. mori encodes a protein of 565 amino acids with a calculated molecular mass of 63.4 kDa and the H. cunea chitinase cDNA encodes a protein of 553 amino acids with a calculated molecular mass of 62.0 kDa. Amino acid alignment of the two chitinases revealed 75% homology and 77-80% with M. sexta chitinase. The putative cleavage site of the signal peptide was between amino acid residues 20 and 21 for both chitinases. There were three potential N-glycosylation sites in the chitinase of B. mori at the amino acid residues 86-89, NFTS, 304-307, NATG, 398-101, NYTV, whereas two potential N-glycosylation sites were present at the amino acid residues 86-89, NFTA and 304-307, NATG, in that of H. cunea. Southern blot analysis of total genomic DNA suggested that the B. mori genome has only one chitinase gene detectable by the cDNA probe and the H. cunea genome has one or two chitinase gene copies. Northern analysis indicated that gene expression was up-regulated during the molting process, larval-pupal transformation and pupal-adult transformation, when enzymatic degradation of cuticle was occurring. (C) 1998 Elsevier Science Ltd. All rights reserved.
Publisher
PERGAMON-ELSEVIER SCIENCE LTD
Issue Date
1998-03
Language
English
Article Type
Article
Keywords

LARVAL-PUPAL TRANSFORMATION; INSECT MOLTING FLUID; MANDUCA-SEXTA L; CHITINOLYTIC ENZYMES; PROTEIN; INTEGUMENT; HYDROLYSIS; EXPRESSION; MECHANISM; SEQUENCE

Citation

INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, v.28, no.3, pp.163 - 171

ISSN
0965-1748
URI
http://hdl.handle.net/10203/77677
Appears in Collection
BS-Journal Papers(저널논문)
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