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

被引：65

作者：

Fujita, Kosuke ^{[1
]}

Shimomura, Kumiko ^{[1
]}

Yamamoto, Kei-ichiro ^{[1
]}

Yamashita, Tetsuro ^{[1
]}

Suzuki, Koichi ^{[1
]}

机构：

[1] Iwate Univ, Fac Agr, Dept Agrobiosci, Morioka, Iwate 0208550, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 345卷 / 01期

基金：

日本学术振兴会;

关键词：

glycoside hydrolase; GH48; chitinase; feeding behavior; insect reproductive diapause;

D O I：

10.1016/j.bbrc.2006.04.126

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：502 / 507

页数：6

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