The skeletal proteome of the coral Acropora millepora: the evolution of calcification by co-option and domain shuffling
Ramos-Silva, Paula, Kaandorp, Jaap, Huisman, Lotte, Marie, Benjamin, Zanella-Cléon, Isabelle, Guichard, Nathalie, Miller, David J., and Marin, Frédéric (2013) The skeletal proteome of the coral Acropora millepora: the evolution of calcification by co-option and domain shuffling. Molecular Biology and Evolution, 30 (9). pp. 2099-2112.
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Abstract
In corals, biocalcification is a major function that may be drastically affected by ocean acidification (OA). Scleractinian corals grow by building up aragonitic exoskeletons that provide support and protection for soft tissues. Although this process has been extensively studied, the molecular basis of biocalcification is poorly understood. Notably lacking is a comprehensive catalog of the skeleton-occluded proteins—the skeletal organic matrix proteins (SOMPs) that are thought to regulate the mineral deposition. Using a combination of proteomics and transcriptomics, we report the first survey of such proteins in the staghorn coral Acropora millepora. The organic matrix (OM) extracted from the coral skeleton was analyzed by mass spectrometry and bioinformatics, enabling the identification of 36 SOMPs. These results provide novel insights into the molecular basis of coral calcification and the macroevolution of metazoan calcifying systems, whereas establishing a platform for studying the impact of OA at molecular level. Besides secreted proteins, extracellular regions of transmembrane proteins are also present, suggesting a close control of aragonite deposition by the calicoblastic epithelium. In addition to the expected SOMPs (Asp/Glu-rich, galaxins), the skeletal repertoire included several proteins containing known extracellular matrix domains. From an evolutionary perspective, the number of coral-specific proteins is low, many SOMPs having counterparts in the noncalcifying cnidarians. Extending the comparison with the skeletal OM proteomes of other metazoans allowed the identification of a pool of functional domains shared between phyla. These data suggest that co-option and domain shuffling may be general mechanisms by which the trait of calcification has evolved.
| Item ID: | 29508 |
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| Item Type: | Article (Research - C1) |
| ISSN: | 1537-1719 |
| Keywords: | biomineralization, calcium carbonate skeleton, scleractinian, proteomics, evolution |
| Additional Information: | © The Author 2013. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
| Funders: | European Union Seventh Framework Programme (EU FP7) |
| Projects and Grants: | EU FP7 Marie Curie Initial Training Network BIOMINTEC PITN-GA-2008-215507, EU FP7 Knowledge Based Bio-Economy project BioPreDyn grant 289434, ANR project ACCRO-EARTH, ref. BLAN06-2_159971, COST project TD0903 |
| Date Deposited: | 25 Sep 2013 05:25 |
| FoR Codes: | 06 BIOLOGICAL SCIENCES > 0601 Biochemistry and Cell Biology > 060109 Proteomics and Intermolecular Interactions (excl Medical Proteomics) @ 50% 06 BIOLOGICAL SCIENCES > 0604 Genetics > 060408 Genomics @ 20% 06 BIOLOGICAL SCIENCES > 0604 Genetics > 060409 Molecular Evolution @ 30% |
| SEO Codes: | 97 EXPANDING KNOWLEDGE > 970106 Expanding Knowledge in the Biological Sciences @ 100% |
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