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- Publisher
- Springer Journals
- Copyright
- Copyright © 2011 by Springer-Verlag
- Subject
- Life Sciences; Neurobiology; Proteomics; Life Sciences, general; Biochemical Engineering; Analytical Chemistry; Biochemistry, general
- ISSN
- 0939-4451
- eISSN
- 1438-2199
- DOI
- 10.1007/s00726-011-0932-0
- pmid
- 21590302
- Publisher site
- See Article on Publisher Site
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.
Journal
Amino Acids – Springer Journals
Published: May 18, 2011