Genomic dynamics of brown trout populations released to a novel environment

Population translocations occur for a variety of reasons, from displacement due to climate change to human‐induced transfers. Such actions have adverse effects on genetic variation and understanding their microevolutionary consequences requires monitoring. Here, we return to an experimental release of brown trout (Salmo trutta) in order to monitor the genomic effects of population translocations. In 1979, fish from each of two genetically (F _ST = 0.16) and ecologically separate populations were simultaneously released, at one point in time, to a lake system previously void of brown trout. Here, whole‐genome sequencing of pooled DNA (Pool‐seq) is used to characterize diversity within and divergence between the introduced populations and fish inhabiting two lakes downstream of the release sites, sampled 30 years later (c. 5 generations). Present results suggest that while extensive hybridization has occurred, the two introduced populations are unequally represented in the lakes downstream of the release sites. One population, which is ecologically resident in its original habitat, mainly contributes to the lake closest to the release site. The other population, migratory in its natal habitat, is genetically more represented in the lake further downstream. Genomic regions putatively under directional selection in the new habitat are identified, where allele frequencies in both established populations are more similar to the introduced population stemming from a resident population than the migratory one. Results suggest that the microevolutionary consequences of population translocations, for example, hybridization and adaptation, can be rapid and that Pool‐seq can be used as an initial tool to monitor genome‐wide effects.     

Pathways mediating the nuclear import of histones H3 and H4 in yeast.

The correct assembly of chromatin is necessary for the maintenance of genomic stability in eukaryotic cells. A critical step in the assembly of new chromatin is the cell cycle-regulated synthesis and nuclear import of core histones. Here we demonstrate that the nuclear import pathway of histones H3 and H4 is mediated by at least two karyopherins/importins, Kap123p and Kap121p. Cytosolic H4 is found associated with Kap123p and H3. Kap121p is also present in the H4-PrA-associated fractions, albeit in lesser amounts than Kap123p, suggesting that this Kap serves as an additional import receptor. We further demonstrate that cytosolic Kap123p is associated with acetylated H3 and H4. H3 and H4 each contain a nuclear localization signal (NLS) in their amino-terminal domains. These amino-terminal domains were found to be essential for the nuclear accumulation of H3 and H4-green fluorescent protein reporters. Each NLS mediated direct binding to Kap123p and Kap121p, and decreased nuclear accumulation of H3 and H4 NLS-green fluorescent protein reporters was observed in specific kap mutant strains. H3 and H4 are the first histones to be assembled onto DNA, and these results show that their import is mediated by at least two import pathways.     

Acetyl-<Emphasis Type="SmallCaps">l</Emphasis>-Carnitine Attenuates Arsenic-Induced Oxidative Stress and Hippocampal Mitochondrial Dysfunction

Augmentation of mitochondrial oxidative stress through activating a series of deadly events has implicated as the main culprit of arsenic toxicity and therapeutic approaches based on improving mitochondrial function hold a great promise for attenuating the arsenic-induced toxicity. Acetyl-l-carnitine (ALC) through balancing the coenzyme A (CoA)/acyl-CoA ratio plays an important role in mitochondrial metabolism and thereby can help protect hippocampal neurons from oxidative damage. In the present study, we aimed to explore the effect of arsenic interactions on the mitochondrial function in the hippocampus of rats. Rats were randomly divided into five groups of control (distilled water), sodium arsenite (NaAsO₂, 20 mg/kg), and co-treatment of NaAsO₂ with various doses of ALC in three groups (100, 200, 300 mg/kg) and were treated orally for 21 consecutive days. Our results point out that arsenic exposure caused oxidative stress in rats’ hippocampus, which led to the reactive oxygen species (ROS) generation, mitochondrial swelling, the collapse of the mitochondrial membrane potential, and release of cytochrome c. It also altered Bcl-2/Bax expression ratio and increased caspase-3 and caspase-9 activities. Furthermore, arsenic exposure via activation of NF-κB and microglia increased inflammation. ALC could concentration-dependently counteract the arsenic-induced oxidative stress, modulate the antioxidant defense capacity, and improve mitochondrial functions. In addition, ALC decreased the expression of both death-associated proteins and of inflammatory markers. These findings indicate that ALC improved the arsenic-induced hippocampal mitochondrial dysfunction which underlines the importance of ALC in providing a possible therapeutic strategy for the prevention of arsenic-induced neurodegeneration.     

Join queries optimization in the distributed databases using a hybrid multi-objective algorithm

Cluster Computing - In the distributed database systems, the relations needed by a query can be kept in several locations. This process significantly increases potential corresponding Query...     

Recessive hyperekplexia mutations of the glycine receptor α1 subunit affect cell surface integration and stability

The human neurological disorder hyperekplexia is frequently caused by recessive and dominant mutations of the glycine receptor α1 subunit gene, GLRA1 . Dominant forms are mostly attributed to amino acid substitutions within the ion pore or adjacent loops, resulting in altered channel properties. Here, the biogenesis of glycine receptor α1 subunit mutants underlying recessive forms of hyperekplexia was analyzed following recombinant expression in HEK293 cells. The α1 mutant S231R resulted in a decrease of surface integrated protein, consistent with reduced maximal current values. Decreased maximal currents shown for the recessive α1 mutant I244N were associated with protein instability, rather than decreased surface integration. The recessive mutants R252H and R392H encode exchanges of arginine residues delineating the intracellular faces of transmembrane domains. After expression, the mutant R252H was virtually absent from the cell surface, consistent with non-functionality and the importance of the positive charge for membrane integration. Surface expression of R392H was highly reduced, resulting in residual chloride conductance. Independent of the site of the mutation within the α1 polypeptide, metabolic radiolabelling and pulse chase studies revealed a shorter half-life of the full-length α1 protein for all recessive mutants as compared to the wild-type. Treatment with the proteasome blocker, lactacystin, significantly increased the accumulation of α1 mutants in intracellular membranes. These observations indicated that the recessive α1 mutants are recognized by the endoplasmatic reticulum control system, and degraded via the proteasome pathway. Thus, the lack of glycinergic inhibition associated with recessive hyperekplexia may be attributed to sequestration of mutant subunits within the endoplasmatic reticulum quality control system.