Testis-specific glyceraldehyde-3-phosphate dehydrogenase: origin and evolution

<p>Abstract</p> <p>Background</p> <p>Glyceraldehyde-3-phosphate dehydrogenase (GAPD) catalyses one of the glycolytic reactions and is also involved in a number of non-glycolytic processes, such as endocytosis, DNA excision repair, and induction of apoptosis. Mammals are known to possess two homologous GAPD isoenzymes: GAPD-1, a well-studied protein found in all somatic cells, and GAPD-2, which is expressed solely in testis. GAPD-2 supplies energy required for the movement of spermatozoa and is tightly bound to the sperm tail cytoskeleton by the additional N-terminal proline-rich domain absent in GAPD-1. In this study we investigate the evolutionary history of GAPD and gain some insights into specialization of GAPD-2 as a testis-specific protein.</p> <p>Results</p> <p>A dataset of GAPD sequences was assembled from public databases and used for phylogeny reconstruction by means of the Bayesian method. Since resolution in some clades of the obtained tree was too low, syntenic analysis was carried out to define the evolutionary history of GAPD more precisely. The performed selection tests showed that selective pressure varies across lineages and isoenzymes, as well as across different regions of the same sequences.</p> <p>Conclusions</p> <p>The obtained results suggest that GAPD-1 and GAPD-2 emerged after duplication during the early evolution of chordates. GAPD-2 was subsequently lost by most lineages except lizards, mammals, as well as cartilaginous and bony fishes. In reptilians and mammals, GAPD-2 specialized to a testis-specific protein and acquired the novel N-terminal proline-rich domain anchoring the protein in the sperm tail cytoskeleton. This domain is likely to have originated by exonization of a microsatellite genomic region. Recognition of the proline-rich domain by cytoskeletal proteins seems to be unspecific. Besides testis, GAPD-2 of lizards was also found in some regenerating tissues, but it lacks the proline-rich domain due to tissue-specific alternative splicing.</p

Modeling of Spray System Operation under Hydrogen and Steam Emissions in NPP Containment during Severe Accident

The paper describes one of the variants of mathematical models of a fluid dynamics process inside the containment, which occurs in the conditions of operation of spray systems in severe accidents at nuclear power plant. The source of emergency emissions in this case is the leak of the coolant or rupture at full cross-section of the main circulating pipeline in a reactor building. Leak or rupture characteristics define the localization and the temporal law of functioning of a source of emergency emission (or accrued operating) of warmed up hydrogen and steam in the containment. Operation of this source at the course of analyzed accident models should be described by the assignment of the relevant Dirichlet boundary conditions. Functioning of the passive autocatalytic recombiners of hydrogen is described in the form of the complex Newton boundary conditions

Gymnophrys cometa and Lecythium sp. are core Cercozoa : evolutionary implications

Recent phylogenetic analyses based on different molecular markers have revealed the existence of the Cercozoa, a group of protists including such morphologically diverse taxa as the cercomonad flagellates, the euglyphid testate filose amoebae, the chloroplast-bearing chlorarachniophytes, and the plasmodiophorid plant pathogens. Molecular data also indicate a close relationship between Cercozoa and Foraminifera (Granuloreticulosea). Little is known, however, about the origin of both groups and their phylogenetic relationships. Here we present the complete small-subunit ribosomal RNA (SSU rRNA) sequence of Gymnophrys cometa, formerly included in the athalamid Granuloreticulosea, as well as that of the test-bearing filose amoeba Lecythium sp. Our study shows that the two organisms clearly belong to the Cercozoa, and indicates that Gymnophrys is not closely related to Foraminifera, supporting the view that Granuloreticulosea sensu lato do not form a natural assemblage. Phylogenetic analyses including most available SSU rRNA sequences from Cercozoa suggest that a rigid, external cell envelope appeared several times independently during the evolution of the group. Furthermore, our results bring additional evidence for the wide morphological variety among Cercozoa, which now also include protists bearing granular pseudopodia and exhibiting mitochondria with flattened cristae

The twilight of Heliozoa and rise of Rhizaria, an emerging supergroup of amoeboid eukaryotes

Recent molecular phylogenetic studies revealed the extraordinary diversity of single-celled eukaryotes. However, the proper assessment of this diversity and accurate reconstruction of the eukaryote phylogeny are still impeded by the lack of molecular data for some major groups of easily identifiable and cultivable protists. Among them, amoeboid eukaryotes have been notably absent from molecular phylogenies, despite their diversity, complexity, and abundance. To partly fill this phylogenetic gap, we present here combined small-subunit ribosomal RNA and actin sequence data for the three main groups of “Heliozoa” (Actinophryida, Centrohelida, and Desmothoracida), the heliozoan-like Sticholonche, and the radiolarian group Polycystinea. Phylogenetic analyses of our sequences demonstrate the polyphyly of heliozoans, which branch either as an independent eukaryotic lineage (Centrohelida), within stramenopiles (Actinophryida), or among cercozoans (Desmothoracida), in broad agreement with previous ultrastructure-based studies. Our data also provide solid evidence for the existence of the Rhizaria, an emerging supergroup of mainly amoeboid eukaryotes that includes desmothoracid heliozoans, all radiolarians, Sticholonche, and foraminiferans, as well as various filose and reticulose amoebae and some flagellates