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

Anderluh, G.; Podlesek, Z.; Macek, P.

Biochimica et Biophysica Acta 1476(2): 372-376

2000


ISSN/ISBN: 0006-3002
PMID: 10669802
DOI: 10.1016/s0167-4838(99)00237-x
Accession: 013071021

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Abstract
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.