The larval shells of the marine bivalves Mercenaria mercenaria and Crassostrea gigas are investigated by polarized light microscopy, infrared spectroscopy, Raman imaging spectroscopy, and scanning electron microscopy. Both species contain similar shell ultrastructures. We show that larval shells contain amorphous calcium carbonate (ACC), in addition to aragonite. The aragonite is much less crystalline than nonbiogenic aragonite. We further show that the initially deposited mineral phase is predominantly ACC that subsequently partially transforms into aragonite. The postset juvenile shell, as well as the adult shell of Mercenaria also contains aragonite that is less crystalline than nonbiogenic aragonite. We conclude that ACC fulfills an important function in mollusc larval shell formation. It is conceivable that ACC may also be involved in adult shell formation.
Almost all mineralized tissues contain proteins that are unusually acidic. As they are also often intimately associated with the mineral phase, they are thought to fulfill important functions in controlling mineral formation. Relatively little is known about these important proteins, because their acidic nature causes technical difficulties during purification and characterization procedures. Much effort has been made to overcome these problems, particularly in the study of mollusk-shell formation. To date about 16 proteins from mollusk-shell organic matrices have been sequenced, but only two are unusually rich in aspartic and glutamic acids. Here we screened a cDNA library made from the mRNA of the shell-forming cells of a bivalve, Atrina rigida, using probes for short Asp-containing repeat sequences, and identified ten different proteins. Using more specific probes designed from one subgroup of conserved sequences, we obtained the full sequences of a family of seven aspartic acid-rich proteins, which we named "Asprich"; a subfamily of the unusually acidic shell-matrix proteins. Polyclonal antibodies raised against a synthetic peptide of the conserved acidic1 domain of these proteins reacted specifically with the matrix components of the calcitic prismatic layer, but not with those of the aragonitic nacreous layer. Thus the Asprich proteins are constituents of the prismatic layer shell matrix. We can identify different domains within these sequences, including a signal peptide characteristic of proteins destined for extracellular secretion, a conserved domain rich in aspartic acid that contains a sequence very similar to the calcium-binding domain of Calsequestrin, and another domain rich in aspartic acid, that varies between the seven sequences. We also identified a domain with DEAD repeats that may have Mg-binding capabilities. Although we do not know, as yet, the function of these proteins, their generally conserved sequences do indicate that they might well fulfill basic functions in shell formation.
Indigenous populations of the Americas experienced high mortality rates during the early contact period as a result of infectious diseases, many of which were introduced by Europeans. Most of the pathogenic agents that caused these outbreaks remain unknown. Through the introduction of a new metagenomic analysis tool called MALT, applied here to search for traces of ancient pathogen DNA, we were able to identify Salmonella enterica in individuals buried in an early contact era epidemic cemetery at Teposcolula-Yucundaa, Oaxaca in southern Mexico. This cemetery is linked, based on historical and archaeological evidence, to the 1545-1550 CE epidemic that affected large parts of Mexico. Locally, this epidemic was known as 'cocoliztli', the pathogenic cause of which has been debated for more than a century. Here, we present genome-wide data from ten individuals for Salmonella enterica subsp. enterica serovar Paratyphi C, a bacterial cause of enteric fever. We propose that S. Paratyphi C be considered a strong candidate for the epidemic population decline during the 1545 cocoliztli outbreak at Teposcolula-Yucundaa.
mere presence of the activation domain because of its small size (about 6% of the total mass) relative to the CRSP complex. Further, we have mapped the VP16 and SREBP-1a binding sites to comparatively small and distinct regions on the CRSP complex. This provides direct evidence that only a limited number (one or perhaps two) of CRSP subunits are targeted by a particular activator. Because VP16-CRSP and SREBP-CRSP are conformationally distinct in regions distal to the activator binding sites, we suggest that activator binding may induce longrange conformational changes. Thus, different protein surfaces in CRSP are likely exposed as a consequence of activator binding.The conformational flexibility of the CRSP coactivator may have important implications for its mechanism of action. CRSP and its related coactivator complexes appear to be generally required for transcription and are targeted by a diverse array of regulatory proteins (22). Interestingly, different transcription activators can target different subunits of the CRSP complex (3, 9,20,21). Thus, despite binding the same coactivator complex, regulatory proteins may impart promoter-specific functions that may be dependent on CRSP conformation. For example, specific activator-induced CRSP conformations may regulate binding and recruitment of additional activators or cofactors to the preinitiation complex (Fig. 5). Furthermore, these conformational changes may trigger other (as yet undiscovered) enzymatic activities within the CRSP coactivator. Indeed, adopting a number of activator-dependent conformations may enable CRSP to perform more specialized roles in transcriptional activation. Elucidation of these roles will be an important subject of future work. We used the natural abundance of stable isotopes (carbon and hydrogen) in the feathers of a neotropical migrant songbird to determine where birds from particular breeding areas spend the winter and the extent to which breeding populations mix in winter quarters. We show that most birds wintering on western Caribbean islands come from the northern portion of the species' North American breeding range, whereas those on more easterly islands are primarily from southern breeding areas. Although segregated by breeding latitude, birds within local wintering areas derive from a wide range of breeding longitudes, indicating considerable population mixing with respect to breeding longitude. These results are useful for assessing the effects of wintering habitat loss on breeding population abundances and for predicting whether the demographic consequences will be concentrated or diffuse.In recent decades, many species of neotropical migrant birds have shown marked changes in abundance-both increases and de-
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