The B proteins secreted by the tubular accessory sex glands of the male mealworm beetle, Tenebrio molitor, have sequence similarity to moth pheromone-binding proteins.
The B proteins secreted by the tubular accessory sex glands of the male mealworm beetle, Tenebrio molitor, have sequence similarity to moth pheromone-binding proteins.
复制标题
雄性黄粉虫的管状副性腺分泌的 B 蛋白与蛾信息素结合蛋白具有序列相似性。
DOI：
10.1016/0965-1748(94)00085-v
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发表时间：
1995
影响因子：
3.8
通讯作者：
Happ,GM
中科院分区：
文献类型：
--
作者：
Paesen,GC;Happ,GM
B蛋白是成虫、雄虫管状副腺分泌的四种主要蛋白质组之一。它们是表观分子质量为18.8 kDa的酸性蛋白质。本文给出了两种几乎相同的B蛋白的推导氨基酸序列，分别命名为B1和B2。成熟蛋白全长118个氨基酸。它们含有11个(B2)或12个(B1)可能的磷酸化位点，富含谷氨酸(16%)。凝集素结合实验表明存在天冬酰胺连接的碳水化合物。据预测，B蛋白的二级结构几乎完全是a螺旋的。B蛋白与飞蛾和果蝇中的一组信息素和气味结合蛋白显示出显著的序列相似性，表明它是脂类的载体蛋白。
B proteins represent one of the four major protein groups secreted by the tubular accessory glands of adult, male mealworm beetles. They are acidic proteins with an apparent molecular mass of 18.8 kDa. In this paper we present the deduced amino-acid sequences of two, almost identical B proteins, termed B1 and B2. The mature proteins are 118 amino acids long. They contain 11 (B2) or 12 (B1) possible phosphorylation sites and are rich in glutamic acid (16%). Lectin binding experiments indicate the presence of asparagine linked carbohydrate. The secondary structure of the B proteins is predicted to be almost completely a-helical. The B proteins show significant sequence resemblance to a group of pheromone- and odorant-binding proteins in moths and Drosophila, suggesting a role as carrier proteins for lipids.