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

The skeletal proteome of the coral Acropora millepora: the evolution of calcification by co-option and domain shuffling.
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DOI:
10.1093/molbev/mst109
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发表时间:
2013-09
影响因子:
10.7
通讯作者:
Marin F
Marin F
中科院分区:
生物学1区
文献类型:
--
作者:
Ramos-Silva P;Kaandorp J;Huisman L;Marie B;Zanella-Cléon I;Guichard N;Miller DJ;Marin F

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在珊瑚中,生物钙化是一个主要功能,可能会受到海洋酸化(OA)的严重影响。硬珊瑚通过文石外骨骼来生长,文石外骨骼为软组织提供支持和保护。虽然这一过程已被广泛研究,生物钙化的分子基础是知之甚少。值得注意的是,缺乏一个全面的目录的骨骼有机基质蛋白(SOMP),被认为是调节矿物质沉积的蛋白质。使用蛋白质组学和转录组学相结合,我们报告的第一次调查,这种蛋白质的鹿角珊瑚鹿角珊瑚千孔珊瑚。从珊瑚骨骼中提取的有机基质(OM)进行了质谱和生物信息学分析,使36 SOMPs的鉴定。这些结果为珊瑚钙化的分子基础和后生动物钙化系统的宏观进化提供了新的见解,同时为在分子水平上研究OA的影响建立了平台。除了分泌蛋白外,还存在跨膜蛋白的细胞外区域,这表明造釉细胞上皮对文石沉积有密切的控制。除了预期的SOMPs(富含Asp/Glu,半乳糖蛋白)外,骨骼库还包括几种含有已知细胞外基质结构域的蛋白质。从进化的角度来看,珊瑚特有的蛋白质的数量很低,许多SOMP在非钙化刺胞动物中有对应物。扩展与其他后生动物的骨骼OM蛋白质组的比较,允许识别门之间共享的功能域的池。这些数据表明,协同选择和结构域改组可能是钙化特征演变的一般机制。
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.
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