@article {3591,
	title = {Biomineralization of Schlumbergerella floresiana, a significant carbonate-producing benthic foraminifer.},
	journal = {Geobiology},
	volume = {12},
	year = {2014},
	month = {2014 Jul},
	pages = {289-307},
	abstract = {<p>Most foraminifera that produce a shell are efficient biomineralizers. We analyzed the calcitic shell of the large tropical benthic foraminifer Schlumbergerella floresiana. We found a suite of macromolecules containing many charged and polar amino acids and glycine that are also abundant in biomineralization proteins of other phyla. As neither genomic nor transcriptomic data are available for foraminiferal biomineralization yet, de novo-generated sequences, obtained from organic matrices submitted to ms blast database search, led to the characterization of 156 peptides. Very few homologous proteins were matched in the proteomic database, implying that the peptides are derived from unknown proteins present in the foraminiferal organic matrices. The amino acid distribution of these peptides was queried against the uniprot database and the mollusk uniprot database for comparison. The mollusks compose a well-studied phylum that yield a large variety of biomineralization proteins. These results showed that proteins extracted from S.\&nbsp;floresiana shells contained sequences enriched with glycine, alanine, and proline, making a set of residues that provided a signature unique to foraminifera. Three of the de novo peptides exhibited sequence similarities to peptides found in proteins such as pre-collagen-P and a group of P-type ATPases including a calcium-transporting ATPase. Surprisingly, the peptide that was most similar to the collagen-like protein was a glycine-rich peptide reported from the test and spine proteome of sea urchin. The molecules, identified by matrix-assisted laser desorption ionization-time of flight mass spectrometry analyses, included acid-soluble N-glycoproteins with its sugar moieties represented by high-mannose-type glycans and carbohydrates. Describing the nature of the proteins, and associated molecules in the skeletal structure of living foraminifera, can elucidate the biomineralization mechanisms of these major carbonate producers in marine ecosystems. As fossil foraminifera provide important paleoenvironmental and paleoclimatic information, a better understanding of biomineralization in these organisms will have far-reaching impacts.</p>
},
	keywords = {Amino Acid Sequence, Amino Acids, Calcification, Physiologic, Carbonates, Electrophoresis, Polyacrylamide Gel, Foraminifera, Molecular Sequence Data, Monosaccharides},
	issn = {1472-4669},
	doi = {10.1111/gbi.12085},
	author = {Sabbatini, A and Bedouet, L and Marie, A and Bartolini, A and Landemarre, L and Weber, M X and Gusti Ngurah Kade Mahardika, I and Berland, Sophie and Zito, F and V{\'e}nec-Peyr{\'e}, M-T}
}
@article {3430,
	title = {The skeleton of the staghorn coral Acropora millepora: molecular and structural characterization.},
	journal = {PLoS One},
	volume = {9},
	year = {2014},
	month = {2014},
	pages = {e97454},
	abstract = {<p>The scleractinian coral Acropora millepora is one of the most studied species from the Great Barrier Reef. This species has been used to understand evolutionary, immune and developmental processes in cnidarians. It has also been subject of several ecological studies in order to elucidate reef responses to environmental changes such as temperature rise and ocean acidification (OA). In these contexts, several nucleic acid resources were made available. When combined to a recent proteomic analysis of the coral skeletal organic matrix (SOM), they enabled the identification of several skeletal matrix proteins, making A. millepora into an emerging model for biomineralization studies. Here we describe the skeletal microstructure of A. millepora skeleton, together with a functional and biochemical characterization of its occluded SOM that focuses on the protein and saccharidic moieties. The skeletal matrix proteins show a large range of isoelectric points, compositional patterns and signatures. Besides secreted proteins, there are a significant number of proteins with membrane attachment sites such as transmembrane domains and GPI anchors as well as proteins with integrin binding sites. These features show that the skeletal proteins must have strong adhesion properties in order to function in the calcifying space. Moreover this data suggest a molecular connection between the calcifying epithelium and the skeletal tissue during biocalcification. In terms of sugar moieties, the enrichment of the SOM in arabinose is striking, and the monosaccharide composition exhibits the same signature as that of mucus of acroporid corals. Finally, we observe that the interaction of the acetic acid soluble SOM on the morphology of in vitro grown CaCO3 crystals is very pronounced when compared with the calcifying matrices of some mollusks. In light of these results, we wish to commend Acropora millepora as a model for biocalcification studies in scleractinians, from molecular and structural viewpoints.</p>
},
	keywords = {Acetic Acid, Amination, Animals, Anthozoa, Bone and Bones, Calcium Carbonate, Crystallization, Gels, Monosaccharides, Proteins, Solubility, Spectroscopy, Fourier Transform Infrared, Spectrum Analysis, Raman},
	issn = {1932-6203},
	doi = {10.1371/journal.pone.0097454},
	author = {Ramos-Silva, Paula and Kaandorp, Jaap and Herbst, Fr{\'e}d{\'e}ric and Plasseraud, Laurent and Alcaraz, G and Stern, Christine and Corneillat, Marion and Guichard, N and Durlet, Christophe and Gilles Luquet and Marin, F}
}
