Juvenile hormone acid O-methyltransferase in Drosophila melanogaster
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چکیده
منابع مشابه
Juvenile hormone acid O-methyltransferase in Drosophila melanogaster.
Juvenile hormone (JH) acid O-methyltransferase (JHAMT) is the enzyme that transfers a methyl group from S-adenosyl-l-methionine (SAM) to the carboxyl group of JH acids to produce active JHs in the corpora allata. While the JHAMT gene was originally identified and characterized in the silkworm Bombyx mori, no orthologs from other insects have been studied until now. Here we report on the functio...
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Juvenile hormone (JH) is critical for multiple aspects of insect development and physiology. Although roles for the hormone have received considerable study, an understanding of the molecules necessary for JH action in insects has been frustratingly slow to evolve. Methoprene-tolerant (Met) in Drosophila melanogaster fulfills many of the requirements for a hormone receptor gene. A paralogous ge...
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Metabolites of the 6,7,10,11 bisepoxide juvenile hormone III (JHB(3)), and other potential juvenoids, were tested for juvenile hormone activity using early instar or early stage pupae of Drosophila melanogaster. Importantly, methyl farnesoates were tested as they might have JH-like activity on Dipteran juveniles. Larvae were exposed to compounds in medium, or the compounds were applied to white...
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Juvenile hormones (JHs) play key roles in regulating metamorphosis and reproduction in insects. The last two steps of JH synthesis diverge depending on the insect order. In Lepidoptera, epoxidation by a P450 monooxygenase precedes esterification by a juvenile hormone acid methyltransferase (JHAMT). In Orthoptera, Dictyoptera, Coleoptera and Diptera epoxidation follows methylation. The aim of ou...
متن کاملEvidence for a juvenile hormone receptor involved in protein synthesis in Drosophila melanogaster.
The larval fat body of newly eclosed adults of Drosophila melanogaster was found to contain a single major binding protein specific for juvenile hormone (JH). Binding to this protein was saturable, of high affinity, and specific for JH III. The protein has a subunit molecular weight (Mr) of 85,000, as determined by photoaffinity labeling. The same or similar JH-binding protein was found in larv...
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ژورنال
عنوان ژورنال: Insect Biochemistry and Molecular Biology
سال: 2008
ISSN: 0965-1748
DOI: 10.1016/j.ibmb.2008.04.003