A common motif in proparts of Cnidarian toxins and nematocyst collagens and its putative role
A common motif in proparts of Cnidarian toxins and nematocyst collagens and its putative role
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DOI：
10.1016/s0167-4838(99)00237-x
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发表时间：
2000-02-09
期刊：
影响因子：
--
通讯作者：
Macek, P
中科院分区：
文献类型：
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作者：
Anderluh, G;Podlesek, Z;Macek, P
在刺胞动物中，成刺胞细胞含有称为刺胞囊的细胞器，据信这是一种极其复杂的受调节的分泌途径的产物。当成熟时，这些刺痛的细胞器能够储存和释放毒素。我们假设翻译的胞囊蛋白可能包含特定的序列，作为细胞器分选的信号。从海葵Actinia equina中克隆了一种钠通道神经毒素，并将毒素前体序列与包囊胶原、孔形成毒素和离子通道神经毒素的前体序列进行了比较。结果发现，所有分析的序列具有一个高度保守的延伸的9个氨基酸残基结束的Lys-Arg的N-末端的成熟区。(C)2000 Elsevier Science B. V.保留所有权利。
In Cnidarians, cnidoblast cells contain organelles called cnidocysts, which are believed to be the product of an extremely complex regulated secretory pathway. When matured, these stinging organelles are capable of storing and delivering toxins. We hypothesized that translated nematocyst proteins might comprise specific sequences serving as signals in sorting to the organelle. A sodium channel neurotoxin from the sea anemone Actinia equina was cloned and the toxin precursor sequence was compared to those of nematocyst collagens, pore-forming toxins and ion channel neurotoxins. It was found that all the analyzed sequences possess a highly conserved stretch of nine amino acid residues ending with Lys-Arg N-terminally of the mature region. (C) 2000 Elsevier Science B.V. All rights reserved.