A chitinase structurally related to the glycoside hydrolase family 48 is indispensable for the hormonally induced diapause termination in a beetle
A chitinase structurally related to the glycoside hydrolase family 48 is indispensable for the hormonally induced diapause termination in a beetle
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DOI：
10.1016/j.bbrc.2006.04.126
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发表时间：
2006-06-23
影响因子：
3.1
通讯作者：
Suzuki, Koichi
中科院分区：
文献类型：
--
作者：
Fujita, Kosuke;Shimomura, Kumiko;Suzuki, Koichi
糖苷水解酶家族48（家族GH48）的两种蛋白质（APAP I和II）分离自叶甲虫Gastrophysa atrocyanea的活跃成虫。对全长和cDNA进行测序。APAP I的表达和功能进行了详细检查。该蛋白质具有几丁质酶活性，但不具有葡聚糖酶和纤维二糖水解酶活性。它在进食阶段表达，包括用保幼激素激动剂终止滞育的甲虫。通过RNA干扰抑制APAP I的表达阻止了滞育的激素终止。(c)2006年爱思唯尔公司All rights reserved.
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.