Changes in ATPase activity, antioxidant enzymes and proline biosynthesis in yeast Candida guilliermondii NP-4 under X-irradiation.

This study investigates the effects of X-radiation on ATPase activity and antioxidant enzyme activity, particularly enzymes involved in proline biosynthesis, in yeast C. guilliermondii NP-4. Moreover, the study examined the post-irradiation repair processes in these cells. Results showed that X-irradiation at a dose of 300 Gy led to an increase in catalase (CAT) and superoxide dismutase (SOD) activity, as well as, an increase in the CAT/SOD ratio in C. guilliermondii NP-4. The repair of radiation-induced damage requires a substantial amount of energy, resulting in an increased demand for ATP in the irradiated and repaired yeasts. Consequently, the total and FoF1-ATPase activity in yeast homogenates and mitochondria increased after X-irradiation and post-irradiation repair. It was showed an increase in the activity of proline biosynthesis enzymes (ornithine transaminase and proline-5-carboxylate reductase) in X-irradiated C. guilliermondii NP-4, which remained elevated even after post-irradiation repair. As a result, the proline levels in X-irradiated and repaired yeasts were higher than those in non-irradiated cells. These findings suggest that proline may have a radioprotective effect on X-irradiated C. guilliermondii NP-4 yeasts. Taken together this study provides insights into the effects of X-radiation on ATPase activity, antioxidant enzyme activity, and proline biosynthesis in C. guilliermondii NP-4 yeast cells, highlighting the potential radioprotective properties of proline in X-irradiated yeasts.

Physical model of the nuclear membrane permeability mechanism.

Nuclear cytoplasmic transport is mediated by many receptors that recognize specific nuclear localization signals on proteins and RNA and transport these substrates through nuclear pore complexes. Facilitated diffusion through nuclear pore complexes requires the attachment of transport receptors. Despite the relatively large tunnel diameter, some even small proteins (less than 20-30 kDa), such as histones, pass through the nuclear pore complex only with transport receptors. Over several decades, considerable material has been accumulated on the structure, architecture, and amino acid composition of the proteins included in this complex and the sequence of many receptors. We consider the data available in the literature on the structure of the nuclear pore complex and possible mechanisms of nuclear-cytoplasmic transport, applying the theory of electrostatic interactions in the context of our data on changes in the electrokinetic potential of nuclei and our previously proposed physical model of the mechanism of facilitated diffusion through the nuclear pore complex (NPC). According to our data, the main contribution to the charge of the nuclear membrane is made by anionic phospholipids, which are part of both the nuclear membrane and the nuclear matrix, which creates a potential difference between them. The nuclear membrane is a four-layer phospholipid dielectric, so the potential vector can only pass through the NPC, creating an electrostatic funnel that "pulls in" the positively charged load-NLS-NTR trigger complexes. Considering the newly obtained data, an improved model of the previously proposed physical model of the mechanism of nuclear-cytoplasmic transport is proposed. This model considers the contribution of electrostatic fields to the transportation speed when changing the membrane's thickness in the NPC basket at a higher load.

Newly Isolated Acidithiobacillus sp. Ksh From Kashen Copper Ore: Peculiarities of EPS and Colloidal Exopolysaccharide.

A novel strain of an iron- and sulfur-oxidizing bacterium was isolated from a natural biotope at Kashen copper ore (Martakert Province, Republic of Artsakh). The strain is able to grow and oxidize ferrous ions in the range of pH 1.4-2.6 with optimal pH 2.0. The optimal temperature for growth is 35°C. Acidithiobacillus sp. Ksh has shown the highest activity for pyrite oxidation among other strains. It also demonstrated high activity in oxidation for copper and copper-gold bearing ores (Armenia). The isolate Acidithiobacillus sp. Ksh was identified as Acidithiobacillus ferrooxidans based on phylogenetic and physiological studies. Comparative studies of EPS production by cells grown on ferrous ions or pyrite were carried out. The chemical composition of capsular and colloidal EPS produced by Acidithiobacillus (At.) ferrooxidans Ksh were revealed to be proteins and carbohydrates. Exosaccharide produced by At. ferrooxidans Ksh is present mainly as polysaccharide in contrast to Leptospirillum (L.) ferriphilum CC, which is oligosaccharide. The structural difference of colloidal particles of these polysaccharides was due to the degree of hydration of the saccharide molecules.

Comparable antibacterial effects and action mechanisms of silver and iron oxide nanoparticles on Escherichia coli and Salmonella typhimurium.

The current research reports the antibacterial effects of silver (Ag) and citric acid coated iron oxide (Fe3O4) NPs on Escherichia coli wild type and kanamycin-resistant strains, as well as on Salmonella typhimurium MDC1759. NPs demonstrated significant antibacterial activity against these bacteria, but antibacterial effect of Ag NPs is more pronounced at low concentrations. Ag NPs inhibited 60-90% of S. typhimurium and drug-resistant E. coli. The latter is more sensitive to Fe3O4 NPs than wild type strain: the number of bacterial colonies is decreased ~ 4-fold. To explain possible mechanisms of NPs action, H+-fluxes through the bacterial membrane and the H+-translocating FOF1-ATPase activity of bacterial membrane vesicles were studied. N,N'-Dicyclohexylcarbodiimide (DCCD)-sensitive ATPase activity was increased up to ~ 1.5-fold in the presence of Fe3O4 NPs. ATPase activity was not detected by Ag NPs even in the presence of DCCD, which confirms the bactericidal effect of these NPs. The H+-fluxes were changed by NPs and by addition of DCCD. H2 yield was inhibited by NPs; the inhibition by Ag NPs is stronger than by Fe3O4 NPs. NPs showed antibacterial effect in bacteria studied in concentration-dependent manner by changing in membrane permeability and membrane-bound enzyme activity. The FOF1-ATPase is suggested might be a target for NPs.