Structure/function analysis of spinalin, a spine protein of Hydra nematocysts
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 comp...
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| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
15 June 2006
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| In: |
The FEBS journal
Year: 2006, Jahrgang: 273, Heft: 14, Pages: 3230-3237 |
| ISSN: | 1742-4658 |
| DOI: | 10.1111/j.1742-4658.2006.05331.x |
| Online-Zugang: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1111/j.1742-4658.2006.05331.x Verlag, kostenfrei, Volltext: http://onlinelibrary.wiley.com/doi/10.1111/j.1742-4658.2006.05331.x/abstract 
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| Verfasserangaben: | Simon Hellstern, Jörg Stetefeld, Charlotte Fauser, Ariel Lustig, Jürgen Engel, Thomas W. Holstein, Suat Özbek |
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| 245 | 1 | 0 | |a Structure/function analysis of spinalin, a spine protein of Hydra nematocysts |c Simon Hellstern, Jörg Stetefeld, Charlotte Fauser, Ariel Lustig, Jürgen Engel, Thomas W. Holstein, Suat Özbek |
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| 520 | |a 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. | ||
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