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Journal Article

Nowa, a novel protein with minicollagen Cys-rich domains, is involved in nematocyst formation in Hydra

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78335

Lottspeich,  F.
Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Engel, U., Oezbek, S., Engel, R., Petri, B., Lottspeich, F., & Holstein, T. W. (2002). Nowa, a novel protein with minicollagen Cys-rich domains, is involved in nematocyst formation in Hydra. Journal of Cell Science, 115(20), 3923-3934.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6E16-F
Abstract
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.