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doi: 10.1242/10.1242/jcs.00084
Research Article |

1 Institute of Zoology, Darmstadt University of Technology, 64287 Darmstadt,
Germany
2 Department of Biophysical Chemistry, Biozentrum, University of Basel, 4056
Basel, Switzerland
3 Institute of Zoology, University of Munich, 80333 Munich, Germany
4 Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany
* Present address: Department of Cell Biology, Harvard Medical School, Boston,
MA 02115, USA
Author for correspondence (e-mail:
holstein{at}bio.tu-darmstadt.de)
Accepted 1 August 2002
The novel protein Nowa was identified in nematocysts, explosive organelles of Hydra, jellyfish, corals and other Cnidaria. Biogenesis of these organelles is complex and involves assembly of proteins inside a post-Golgi vesicle to form a double-layered capsule with a long tubule. Nowa is the major component of the outer wall, which is formed very early in morphogenesis. The high molecular weight glycoprotein has a modular structure with an N-terminal sperm coating glycoprotein domain, a central C-type lectin-like domain, and an eightfold repeated cysteine-rich domain at the C-terminus. Interestingly, the cysteine-rich domains are homologous to the cysteine-rich domains of minicollagens. We have previously shown that the cysteines of these minicollagen cysteine-rich domains undergo an isomerization process from intra- to intermolecular disulfide bonds, which mediates the crosslinking of minicollagens to networks in the inner wall of the capsule. The minicollagen cysteine-rich domains present in both proteins provide a potential link between Nowa in the outer wall and minicollagens in the inner wall. We propose a model for nematocyst formation that integrates cytoskeleton rearrangements around the post-Golgi vesicle and protein assembly inside the vesicle to generate a complex structure that is stabilized by intermolecular disulfide bonds.
Key words: Minicollagen Cys-rich domain, CTLD, Nematocyst, Microtubules, Assembly
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