A common motif in proparts of Cnidarian toxins and nematocyst collagens and its putative role

被引：50

作者：

Anderluh, G ^{[1
]}

Podlesek, Z ^{[1
]}

Macek, P ^{[1
]}

机构：

[1] Univ Ljubljana, Biotech Fac, Dept Biol, Ljubljana 1000, Slovenia

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2000年 / 1476卷 / 02期

关键词：

Cnidaria; pore-forming toxin; collagen; regulated sorting pathway; sorting signal; sodium channel neurotoxin;

D O I：

10.1016/S0167-4838(99)00237-X

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：

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.

引用

页码：372 / 376

页数：5

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