UV-induced DNA degradation in Aspergillus nidulans cells]

UV-induced DNA degradation was studied in mycellial cells of Aspergillus nidulans wild type and several uvs mutants. It was shown to be an enzymatic specific process which possibly reflects the excision of pyrimidine dimers from UV-damaged DNA. Inhibition of DNA degradation by caffeine and 2,4-dinitrophenol shows the connection between degradation and repair of DNA. Two ways of DNA degradation were found in A. nidulans cells, one of them being glucose dependent and the other--glucose independent. The dependence of DNA degradation on protein synthesis before and after UV-irradiation was demonstrated. The scheme of ways of DNA degradation and its genetic control were suggested on the basis of uvs mutations effect on UV-induced DNA degradation.     

Turning Cellulose Waste Into Electricity: Hydrogen Conversion by a Hydrogenase Electrode

Hydrogen-producing thermophilic cellulolytic microorganisms were isolated from cow faeces. Rates of cellulose hydrolysis and hydrogen formation were 0.2 mM L^-1 h^-1 and 1 mM L^-1 h^-1, respectively. An enzymatic fuel cell (EFC) with a hydrogenase anode was used to oxidise hydrogen produced in a microbial bioreactor. The hydrogenase electrode was exposed for 38 days (912 h) to a thermophilic fermentation medium. The hydrogenase activity remaining after continuous operation under load was 73% of the initial value.     

Prebiotic Syntheses Under Shock in the Water – Formamide – Potassium Bicarbonate – Sodium Hydroxide System

Origins of Life and Evolution of Biospheres - Syntheses under shock in nitrogen bubbled samples of the water – formamide – bicarbonate – sodium hydroxide system at...     

First Data on Vibration Signals in Flies of the Genus Meromyza (Diptera,Chloropidae)

Biology Bulletin - This paper discusses vibration communication in representatives of the genus Meromyza. The frequency range of vibration signals of Meromyza saltatrix (L., 1761) females is 229 to...     

Collection of Arabidopsis thalianaMutants with Altered Sensitivity to Oxidative Stress Inductors

Selective systems for screening Arabidopsis thaliana(L.) Heynh. mutants with altered sensitivity to the oxidative stress (OS) inductors norflurazon (NF), acifluorfen (AF), and plumbagin (PB) were developed and a collection of 28 mutants was obtained. Dwarf and necrotic forms predominated among the NF-tolerant mutants, while pigment mutants and those with changed root morphology prevailed among the AF-tolerant and PB-sensitive mutants, respectively. Genetic and biochemical analysis of certain mutants was performed; quantitative and qualitative changes in the content of superoxide dismutase and peroxidase isoforms have been revealed. These data, complemented by the data on the cross-tolerance (sensitivity) of the mutants to paraquat, indicate a correlation between tolerance to the OS inductors and the functions of antioxidant systems.     

Genetic and biochemical evidence for distinct key functions of two highly divergent GAPDH genes in catabolic and anabolic carbon flow of the cyanobacterium Synechocystis sp. PCC 6803

Cyanobacterial genomes harbour two separate highly divergent glyceraldehyde-3-phosphate dehydrogenase (GAPDH) genes, gap1 and gap2, which are closely related at the sequence level to the nuclear genes encoding cytosolic and chloroplast GAPDH of higher plants, respectively. Genes gap1 and gap2 of the unicellular cyanobacterium Synechocystis sp. PCC 6803 were cloned and sequenced and subsequently inactivated by insertional mutagenesis to understand their metabolic functions. We obtained homozygous gap1^- mutants which have lost the capacity to grow on glucose under dim light while growth on organic acids as well as photosynthetic growth under CO₂ and high light is not impaired. Homozygous gap2^- mutants show the reciprocal phenotype. Under dim light they only grow on glucose but not on organic acids nor do they survive under photosynthetic conditions. Measurements of the anabolic activities (reduction of 1,3-bisphosphoglycerate) in extracts from wild type and mutant cells show that Gap2 is a major enzyme with dual cosubstrate specificity for NAD and NADP, while Gap1 displays a minor NAD-specific GAPDH activity. However, if measured in the catabolic direction (oxidation of glyceraldehyde-3-phosphate) Gap2 activity is very low and increases three- to fivefold after gel filtration of extracts over Sephadex G25. Our results suggest that enzymes Gap1 and Gap2, although coexpressed in cyanobacterial wild-type cells, play distinct key roles in catabolic and anabolic carbon flow, respectively. While Gap2 operates in the photosynthetic Calvin cycle and in non-photosynthetic gluconeogenesis, Gap1 seems to be essential only for glycolytic glucose breakdown, conditions under which the catabolic activity of Gap2 seems to be repressed by a specific low-molecular-weight inhibitor.