A chitinase structurally related to the glycoside hydrolase family 48 is indispensable for the hormonally induced diapause termination in a beetle

Two proteins (APAP I and II) of the glycoside hydrolase family 48 (Family GH48) were isolated from the active adults of the leaf beetle Gastrophysa atrocyanea. Full-length and cDNAs were sequenced. APAP I expression and function were examined in detail. The protein has a chitinase but not a glucanas...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2006-06, Vol.345 (1), p.502-507
Main Authors: Fujita, Kosuke, Shimomura, Kumiko, Yamamoto, Kei-ichiro, Yamashita, Tetsuro, Suzuki, Koichi
Format: Article
Language:English
Subjects:
Animals
Chitinase
Chitinases - metabolism
Chrysomelidae
Coleoptera - drug effects
Coleoptera - physiology
Feeding behavior
Feeding Behavior - drug effects
Feeding Behavior - physiology
GH48
Glycoside hydrolase
Glycoside Hydrolases - metabolism
Insect reproductive diapause
Isoenzymes - metabolism
Juvenile Hormones - pharmacology
Life Cycle Stages - drug effects
Life Cycle Stages - physiology
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Summary:Two proteins (APAP I and II) of the glycoside hydrolase family 48 (Family GH48) were isolated from the active adults of the leaf beetle Gastrophysa atrocyanea. Full-length and cDNAs were sequenced. APAP I expression and function were examined in detail. The protein has a chitinase but not a glucanase and cellobiohydrolase activity. It is expressed in the feeding stages, including beetles whose diapause was terminated with a juvenile hormone agonist. Suppression of the APAP I expression by means of RNA interference prevented the hormonal termination of diapause.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2006.04.126