期刊
CHEMBIOCHEM
卷 12, 期 13, 页码 2033-2043出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201100216
关键词
biomineralization; glycoproteins; organic matrix; pearl oyster; protein structures
资金
- Institut Francais de Recherche pour l'Exploitation de la Mer (French Research Institute for Exploration of the Sea, IFREMER)
- Service de la Perliculture Research and Development Department, Tahiti, French Polynesia
- ANR (Agence National de la Recherche) [BLAN06-2_159971]
The shell of pearl oysters is organized in multiple layers of CaCO3 crystallites packed together in an organic matrix. Relationships between the components of the organic matrix and mechanisms of nacre formation currently constitute the main focus of research into biomineralization. In this study, we characterized the pearlin protein from the oyster Pinctada margaritifera (Pmarg); this shares structural features with other members of a matrix protein family, N14/N16/pearlin. Pmarg pearlin exhibits calcium-and chitin-binding properties. Pmarg pearlin transcripts are distinctively localized in the mineralizing tissue responsible for nacre formation. More specifically, we demonstrate that Pmarg pearlin is localized within the interlamellar matrix of nacre aragonite tablets. Our results support recent models for multidomain matrix protein involvement in nacreous layer formation. We provide evidence here for the existence of a conserved family of nacre-associated proteins in Pteriidae, and reassess the evolutionarily conserved set of biomineralization genes related to nacre formation in this taxa.
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