BackgroundScleractinian corals are currently a focus of major interest because of their ecological importance and the uncertain fate of coral reefs in the face of increasing anthropogenic pressure. Despite this, remarkably little is known about the evolutionary origins of corals. The Scleractinia suddenly appear in the fossil record about 240 Ma, but the range of morphological variation seen in these Middle Triassic fossils is comparable to that of modern scleractinians, implying much earlier origins that have so far remained elusive. A significant weakness in reconstruction(s) of early coral evolution is that deep-sea corals have been poorly represented in molecular phylogenetic analyses.ResultsBy adding new data from a large and representative range of deep-water species to existing molecular datasets and applying a relaxed molecular clock, we show that two exclusively deep-sea families, the Gardineriidae and Micrabaciidae, diverged prior to the Complexa/Robusta coral split around 425 Ma, thereby pushing the evolutionary origin of scleractinian corals deep into the Paleozoic.ConclusionsThe early divergence and distinctive morphologies of the extant gardineriid and micrabaciid corals suggest a link with Ordovician "scleractiniamorph" fossils that were previously assumed to represent extinct anthozoan skeletonized lineages. Therefore, scleractinian corals most likely evolved from Paleozoic soft-bodied ancestors. Modern shallow-water Scleractinia, which are dependent on symbionts, appear to have had several independent origins from solitary, non-symbiotic precursors. The Scleractinia have survived periods of massive climate change in the past, suggesting that as a lineage they may be less vulnerable to future changes than often assumed.
We have studied the oxidation reactions of two polycyclic aromatic hydrocarbons (PAHs), pyrene and
anthracene, attached covalently to silica, indium-doped tin oxide (ITO), and gold surfaces. Attachment of the
PAHs to the substrates was accomplished by established covalent coupling methods. For both pyrene and
anthracene, we find that electrochemical and photochemical oxidation produces first a monohydroxy-PAH
followed by the formation of dihydroxy/dione derivatives. We have used cyclic voltammetry and steady-state excitation and emission spectroscopy to identify the products of the surface reactions. The uniformity
of our results for two chromophores and three different types of substrates demonstrates the generality of our
findings and rules out the involvement of surface enhancement phenomena in these processes.
It has been generally thought that scleractinian corals form purely aragonitic skeletons. We show that a well-preserved fossil coral, Coelosmilia sp. from the Upper Cretaceous (about 70 million years ago), has preserved skeletal structural features identical to those observed in present-day scleractinians. However, the skeleton of Coelosmilia sp. is entirely calcitic. Its fine-scale structure and chemistry indicate that the calcite is primary and did not form from the diagenetic alteration of aragonite. This result implies that corals, like other groups of marine, calcium carbonate-producing organisms, can form skeletons of different carbonate polymorphs.
Fish otoliths, biominerals composed of calcium carbonate with a small amount of organic matrix, are involved in the functioning of the inner ear. Starmaker (Stm) from zebrafish (Danio rerio) was the first protein found to be capable of controlling the formation of otoliths. Recently, a gene was identified encoding the Starmaker-like (Stm-l) protein from medaka (Oryzias latipes), a putative homologue of Stm and human dentine sialophosphoprotein. Although there is no sequence similarity between Stm-l and Stm, Stm-l was suggested to be involved in the biomineralization of otoliths, as had been observed for Stm even before. The molecular properties and functioning of Stm-l as a putative regulatory protein in otolith formation have not been characterized yet. A comprehensive biochemical and biophysical analysis of recombinant Stm-l, along with in silico examinations, indicated that Stm-l exhibits properties of a coil-like intrinsically disordered protein. Stm-l possesses an elongated and pliable structure that is able to adopt a more ordered and rigid conformation under the influence of different factors. An in vitro assay of the biomineralization activity of Stm-l indicated that Stm-l affected the size, shape and number of calcium carbonate crystals. The functional significance of intrinsically disordered properties of Stm-l and the possible role of this protein in controlling the formation of calcium carbonate crystals is discussed.
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