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Penicillium brevicompactum highly tolerated cobalt concentrations of 50, 200, 800 and 1000 ppm both through cell wall and intracellular sequestration - immobilization of the metal on/within the cell wall, cell wall thickness, presence of electron-dense deposits inside vacuoles (thiol peptides sequestering cobalt) and in the cytoplasm (cobalt), and presence of matrixed electron-dense deposits, only at 800 and 1000 ppm, were observed. Increased vacuole formation and plasmolysis were also observed. Fraction number 9 of the cell free extract showed maximum cobalt uptake for all the investigated cobalt concentrations. In this fraction, glutathione was only induced at 500, 800 and 1000 ppm. Maximum glutathione concentration supported maximum cobalt uptake at 800 ppm. Low molecular weight protein profiles of fraction number 9 revealed that the presence of cobalt induced the appearance of new proteins that were not detected in the same fraction of the control. These low molecular weight peptides (12-5 KDa) suggest the production of Co-metallothioneins. This is the first report of cobalt-induced glutathione by P. brevicompactum and suggests the possible production of phytochelatins.
We analyzed DNA damage, mitotic activity and polyploidization in Crepis capillaris callus cells during short- and long-term in vitro culture, and the influence of plant growth regulators on these processes. Changes in the concentration of growth regulators altered the stability of callus. The level of DNA damage was highly dependent on the growth regulator composition of the medium. Cytokinin at high concentrations damaged DNA in the absence of auxin. Short- and long-term callus differed in sensitivity to growth regulators. Mitotic activity changed when callus was transferred to medium with modified growth regulators. Callus cell nuclear DNA content increased with age and in response to plant growth regulators. Hormones played a role in the genetic changes in C. capillaris callus culture. We demonstrated the usefulness of C. capillaris callus culture as a model for analyzing the effect of culture conditions, including plant growth regulators, on genetic stability.
We analyzed DNA lesions produced by H2O2 under low iron conditions, the cross adaptive response and the synergistic lethal effect produced by iron chelator-o-phenanthroline, using different Escherichia coli mutants deficient in DNA repair mechanisms. At normal iron levels the lesions produced by H2O2 are repaired mainly by the exonuclease III protein. Under low iron conditions we observed that the Fpg and UvrA proteins as well as SOS and OxyR systems participate in the repair of these lesions. The lethal effect of H2O2 is strengthened by o-phenanthroline if both compounds are added simultaneously to the culture medium. This phenomenon was observed in the wild type cells and in the xthA mutant (hypersensitive to H2O2). E. coli cells treated with low concentrations of H2O2 (micromolar) acquire resistance to different DNA damaging agents. Our results indicate also that pretreatment with high (millimolar) H2O2 concentrations protects cells against killing, by UV and this phenomenon is independent of the SOS system, but dependent on RecA and UvrA proteins. H2O2 induces protection against lethal and mutagenic effects of N-methyl-N'-nitro-N-nitrosoguanidine (MNNG). H2O2 also protects the cells against killing, by cumene hydroperoxide, possibly with the participation of Ahp protein.
Plant calcium pumps, similarly to animal Ca2+ pumps, belong to the superfamily of P-type ATPases comprising also the plasma membrane H+-ATPase of fungi and plants, Na+/K+ ATPase of animals and H+/K+ ATPase of mammalian gastric mucosa. According to their sensitivity to calmodulin the plant Ca2+-ATPases have been divided into two subgroups: type IIA (homologues of animal SERCA) and type IIB (homologues of animal PMCA). Regardless of the similarities in a protein sequence, the plant Ca2+ pumps differ from those in animals in their cellular localization, structure and sensitivity to inhibitors. Genomic investigations revealed multiplicity of plant Ca2+-ATPases; they are present not only in the plasma membranes and ER but also in membranes of most of the cell compartments, such as vacuole, plastids, nucleus or Golgi apparatus. Studies using yeast mutants made possible the functional and biochemical characterization of individual plant Ca2+- -ATPases. Plant calcium pumps play an essential role in signal transduction pathways, they are responsible for the regulation of [Ca2+] in both cytoplasm and endomembrane comparE ments. These Ca2+-ATPases appear to be involved in plant adaptation to stress conditions, like salinity, chilling or anoxia.
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