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

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.

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Genre: Journal Article
Alternative Title : J. Cell Sci.

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 Creators:
Engel, U., Author
Oezbek, S., Author
Engel, R., Author
Petri, B., Author
Lottspeich, F.1, Author           
Holstein, T. W., Author
Affiliations:
1Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565158              

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Free keywords: minicollagen Cys-rich domain; CTLD; nematocyst; microtubules; assembly
 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.

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Language(s): eng - English
 Dates: 2002-10-15
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 39012
ISI: 000179179800008
 Degree: -

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Title: Journal of Cell Science
  Alternative Title : J. Cell Sci.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 115 (20) Sequence Number: - Start / End Page: 3923 - 3934 Identifier: ISSN: 0021-9533