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Cloning and characterization of the Bombyx mori ecdysone oxidase.
- Source :
-
Archives of insect biochemistry and physiology [Arch Insect Biochem Physiol] 2011 Sep; Vol. 78 (1), pp. 17-29. Date of Electronic Publication: 2011 Jun 15. - Publication Year :
- 2011
-
Abstract
- The physiological titer of molting hormones in insects depends on relative activities of synthesis and degradation pathways. Ecdysone oxidase (EO) is a key enzyme in the inactivation of ecdysteroid. However, there are only a few reports on ecdysteroid inactivation and its enzymes in silkworm. In this study, we cloned and characterized the Bombyx mori EO (BmEO). The BmEO cDNA contains an ORF of 1,695 bp and the deduced protein sequence contains 564 amino acid residues. The deduced protein sequence contains two functional domains of glucose-methanol-choline oxidoreductase in N-terminal and C-terminal. Comparing the expression levels of BmEO in different tissues, high transcription was mainly present in hemocytes. Reduced expression of this enzyme is expected to lead to pathological accumulation of ecdysone in the hemolymph of silkworm larvae or pupae. Our data show that RNA inference of BmEO transcripts resulted in the accumulation of ecdysteroid and death of larvae or pupae. We infer that EO is a crucial element in the physiology of insect development.<br /> (© 2011 Wiley Periodicals, Inc.)
- Subjects :
- 3-Hydroxysteroid Dehydrogenases analysis
3-Hydroxysteroid Dehydrogenases chemistry
Amino Acid Sequence
Animals
Base Sequence
Bombyx genetics
Bombyx growth & development
Cloning, Molecular
DNA, Complementary genetics
Hemocytes enzymology
Hemolymph
Larva enzymology
Larva growth & development
Pupa enzymology
Pupa growth & development
RNA Interference
Sequence Analysis, DNA
Sequence Analysis, Protein
3-Hydroxysteroid Dehydrogenases genetics
Bombyx enzymology
Ecdysteroids metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1520-6327
- Volume :
- 78
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Archives of insect biochemistry and physiology
- Publication Type :
- Academic Journal
- Accession number :
- 21678487
- Full Text :
- https://doi.org/10.1002/arch.20436