Sponges (Porifera) represent the evolutionary oldest multicellular animals. They are provided with the basic molecules involved in cell-cell and cell-matrix interactions. We report here the isolation and characterization of a complementary DNA from the sponge Suberites domuncula coding for the sponge homeobox gene, SUBDOIRX-a. The deduced polypeptide with a predicted Mr of 44,375 possesses the highly conserved Iroquois-homeodomain. We applied in situ hybridization to localize Iroquois in the sponge. The expression of this gene is highest in cells adjacent to the canals of the sponge in the medulla region. To study the expression of Iroquois during development, the in vitro primmorph system from S. domuncula was used. During the formation of these three-dimensional aggregates composed of proliferating cells, the expression of Iroquois depends on ferric iron and water current. An increased expression in response to water current is paralleled with the formation of canal-like pores in the primmorphs. It is suggested that Iroquois expression is involved in the formation of the aquiferous system, the canals in sponges and the canal-like structures in primmorphs.

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Tubulin polymerization promoting proteins (TPPPs) constitute a eukaryotic protein family. There are three TPPP paralogs in the human genome, denoted as TPPP1-TPPP3. TPPP1 and TPPP3 are intrinsically unstructured proteins (IUPs) that bind and polymerize tubulin and stabilize microtubules, but TPPP2 does not. Vertebrate TPPPs originated from the ancient invertebrate TPPP by two-round whole-genome duplication; thus, whether the tubulin/microtubule binding function of TPPP1 and TPPP3 is a newly acquired property or was present in the invertebrate orthologs (generally one TPPP per species) has been an open question. To answer this question, we investigated a TPPP from a simple and early branching animal, the sponge Suberites domuncula. Bioinformatics, biochemical, immunochemical, spectroscopic, and electron microscopic data showed that the properties of the sponge protein correspond to those of TPPP1; namely, it is an IUP that strongly binds tubulin and induces its polymerization, proving that these features of animal TPPPs have been evolutionarily conserved.

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Market demand for scallops has considerably increased in recent decades. Although natural populations of scallops are vulnerable, the queen scallop, Aequipecten opercularis, can represent a possible alternative to at-risk species. The aim of this study was to determine the effect of seawater parameters on the commercial quality, biological indices and nutritional quality of the scallop A. opercularis in 1900 L tanks in ex situ conditions. The condition index (CI) and meat yield (MY) peaked in autumn (89.92% and 40.29%, respectively). The muscle index (MI) showed the highest peak during the winter season (5.96%), while the gonadosomatic index (GSI) (34.06%) peaked in the spring months. Protein content (6.89–9.56 g/100 g), lipids (2.58–2.79 g/100 g) and carbohydrates (0.12–0.33 g/100 g) varied during the study period. Seasonal fluctuations in seawater temperature and pH negatively influenced the CI, MY and protein and lipid content, while positively affecting carbohydrate and moisture content. The most suitable period of the year for the consumption of the scallop A. opercularis was found to be the winter and spring periods, when the scallops achieved their highest nutritional value. It can be stated from this study that queen scallops in the Adriatic Sea have a high nutritional quality and that they can be proposed for higher human consumption.