Characterization of MRNP34, a novel methionine-rich nacre protein from the pearl oysters
| Type | Article | ||||||||||||
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| Date | 2012-05 | ||||||||||||
| Language | English | ||||||||||||
| Author(s) | Marie Benjamin, Joubert Caroline, Belliard Corinne, Tayale Alexandre, Zanella-Cleon Isabelle, Marin Frederic, Gueguen Yannick , Montagnani Caroline |
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| Affiliation(s) | IFREMER, Ctr Oceanolog Pacifique, LBQP, Taravao, Fr Polynesia. Univ Bourgogne, CNRS, UMR 5561, Dijon, France. Univ Lyon 1, CNRS, IBCP, IFR BioSci 128,UMR 5086, F-69365 Lyon, France. |
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| Source | Amino Acids (0939-4451) (Springer), 2012-05 , Vol. 42 , N. 5 , P. 2009-2017 | ||||||||||||
| DOI | 10.1007/s00726-011-0932-0 | ||||||||||||
| WOS© Times Cited | 23 | ||||||||||||
| Keyword(s) | Matrix protein, Methionine-rich, Biomineralization, Mollusc, Nacre, Calcifying mantle | ||||||||||||
| Abstract | Nacre of the Pinctada pearl oyster shells is composed of 98% CaCO3 and 2% organic matrix. The relationship between the organic matrix and the mechanism of nacre formation currently constitutes the main focus regarding the biomineralization process. In this study, we isolated a new nacre matrix protein in P. margaritifera and P. maxima, we called Pmarg- and Pmax-MRNP34 (methionine-rich nacre protein). MRNP34 is a secreted hydrophobic protein, which is remarkably rich in methionine, and which is specifically localised in mineralizing the epithelium cells of the mantle and in the nacre matrix. The structure of this protein is drastically different from those of the other nacre proteins already described. This unusual methionine-rich protein is a new member in the growing list of low complexity domain containing proteins that are associated with biocalcifications. These observations offer new insights to the molecular mechanisms of biomineralization. | ||||||||||||
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