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J. Biol. Chem., Vol. 277, Issue 51, 49200-49204, December 20, 2002

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Structure/Function Relationships in the Minicollagen of Hydra Nematocysts^*

Suat Özbek, Olivier Pertz^§, Martine Schwager, Ariel Lustig, Thomas Holstein^¶, and Jürgen Engel

From the  Department of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland, ^§ Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, and ^¶ Institute of Zoology, Technical University of Darmstadt, Schnittpahnstrasse 10, D-64287 Darmstadt, Germany

The minicollagens found in the inner layer of the Hydra nematocyst walls are the smallest collagens known with 12-16 Gly-X-Y repeats. Minicollagen-1, the best characterized member of this protein family so far, consists of a central collagen triple helix of 12 nm in length flanked at both ends by a polyproline stretch and a conserved cysteine-rich domain. The cysteine-rich tails are proposed to function in the assembly of soluble minicollagen trimers to high molecular structures by a switch of the disulfide linkage from intramolecular to intermolecular bonds. In this study, we investigate the trimeric nature of minicollagen-1 and its capacity to form disulfide-linked polymers in vitro. A fusion protein of minicollagen-1 with maltose-binding protein is secreted as a soluble trimer with only intrachain and no interchain disulfide bridges as confirmed by melting the collagen triple helix under reducing and non-reducing conditions. The conversion of minicollagen-1 trimers to monomers takes place between 40 and 55 °C with the melting point being ~45 °C. Oxidative reshuffling of the minicollagen-1 trimers leads to the formation of high molecular aggregates, which upon reduction show distinct polytrimeric states. Minicollagen trimers in isolated nematocyst capsules proved to be sensitive to SDS and were engaged in polymeric structures with additional cross-links that were resistant to reducing agent.

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