TAILIEUCHUNG - Báo cáo khoa học: Calcite-specific coupling protein in barnacle underwater cement

The barnacle relies for its attachment to underwater foreign substrata on the formation of a multiprotein complex called cement. The 20 kDa cement protein is a component ofMegabalanus rosacement, although its specific function in underwater attachment has not, until now, been known. | ễFEBS Journal Calcite-specific coupling protein in barnacle underwater cement Youichi Mori1 Youhei Urushida1 Masahiro Nakano1 Susumu Uchiyama2 and Kei Kamino1 1 Marine Biotechnology Institute Kamaishi Iwate Japan 2 Department of Biotechnology Graduate Schoolof Engineering Osaka University Japan Keywords adsorption crustacean protein complex sessile organism underwater adhesive Correspondence K. Kamino Marine Biotechnology Institute 3-75-1 Heita Kamaishi Iwate 026-0001 Japan Fax 81 193 26 6592 Tel. 81 193 26 6584 E-mail Database The nucleotide sequence data are available in the DNA Data Bank of Japan under the accession number AB329666 Received 5 July 2007 revised 18 October 2007 accepted 23 October 2007 doi The barnacle relies for its attachment to underwater foreign substrata on the formation of a multiprotein complex called cement. The 20 kDa cement protein is a component of Megabalanus rosa cement although its specific function in underwater attachment has not until now been known. The recombinant form of the protein expressed in bacteria was purified in soluble form under physiological conditions and confirmed to retain almost the same structure as that of the native protein. Both the protein from the adhesive layer of the barnacle and the recombinant protein were characterized. This revealed that abundant Cys residues which accounted for 17 of the total residues were in the intramolecular disulfide form and were essential for the proper folding of the monomeric protein structure. The recombinant protein was adsorbed to calcite and metal oxides in seawater but not to glass and synthetic polymers. The adsorption isotherm for adsorption to calcite fitted the Langmuir model well indicating that the protein is a calcite-specific adsorbent. An evaluation of the distribution of the molecular size in solution by analytical ultracentrifugation indicated that the recombinant protein exists as a monomer in 100 mM to 1 M

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