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

J Cell Sci. 2002 Oct 15;115(Pt 20):3923-34. doi: 10.1242/jcs.00084.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal / metabolism
  • Antigens, Surface / chemistry
  • Antigens, Surface / metabolism
  • Collagen / chemistry*
  • Collagen / metabolism
  • Cysteine / chemistry
  • Disulfides / chemistry
  • Electrophoresis, Gel, Two-Dimensional
  • Escherichia coli / genetics
  • Glycoproteins / chemistry*
  • Glycoproteins / metabolism
  • Glycosylation
  • Hydra / cytology
  • Hydra / metabolism*
  • Hydra / ultrastructure
  • Microtubules / metabolism
  • Microtubules / ultrastructure
  • Models, Biological
  • Molecular Sequence Data
  • Molecular Weight
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Tertiary
  • Protein Transport
  • RNA, Messenger / metabolism
  • Recombinant Proteins / metabolism
  • Repetitive Sequences, Amino Acid
  • Sequence Homology, Amino Acid

Substances

  • Antibodies, Monoclonal
  • Antigens, Surface
  • Disulfides
  • Glycoproteins
  • RNA, Messenger
  • Recombinant Proteins
  • Collagen
  • Cysteine

Associated data

  • GENBANK/AF539862