The skeletal proteome of the coral Acropora millepora: the evolution of calcification by co-option and domain shuffling

• Published in: Molecular Biology and Evolution
• Main Authors: Ramos-Silva, P., Kaandorp, J., Huisman, L., Marie, B., Zanella-Cléon, I., Guichard, N., Miller, D.J., Marin, F.
• Format: Article in Journal/Newspaper
• Language: English
• Published: 2013
• Subjects: Ocean acidification
• Online Access: https://dare.uva.nl/personal/pure/en/publications/the-skeletal-proteome-of-the-coral-acropora-millepora-the-evolution-of-calcification-by-cooption-and-domain-shuffling(f2219f5a-c4ef-40c5-8ae6-cf0867a79167).html; https://doi.org/10.1093/molbev/mst109; https://pure.uva.nl/ws/files/9870180/mst109.pdf

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.