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Structure/function analysis of spinalin, a spine protein of Hydra nematocysts
Author(s) -
Hellstern Simon,
Stetefeld Jörg,
Fauser Charlotte,
Lustig Ariel,
Engel Jürgen,
Holstein Thomas W.,
Özbek Suat
Publication year - 2006
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2006.05331.x
Subject(s) - nematocyst , lernaean hydra , cnidocyte , microbiology and biotechnology , biophysics , chemistry , cysteine , biology , biochemistry , cnidaria , ecology , coral , enzyme
The nematocyst capsules of the cnidarians are specialized explosive organelles that withstand high osmotic pressures of ≈ 15 MPa (150 bar). A tight disulfide network involving cysteine‐rich capsule wall proteins, like minicollagens and nematocyst outer wall antigen, characterizes their molecular composition. Nematocyst discharge leads to the expulsion of a long inverted tubule that was coiled inside the capsule matrix before activation. Spinalin has been characterized as a glycine‐rich, histidine‐rich protein associated with spine structures on the surface of everted tubules. Here, we show that full‐length Hydra spinalin can be expressed recombinantly in HEK293 cells and has the property to form disulfide‐linked oligomers, reflecting its state in mature capsules. Furthermore, spinalin showed a high tendency to associate into dimers in vitro and in vivo . Our data, which show incomplete disulfide connectivity in recombinant spinalin, suggest a possible mechanism by which the spine structure may be linked to the overall capsule polymer.