Programmed cell death - strategy for maintenance cellular organisms homeostasis.

Programmed cell death (PCD) is a cellular suicide process, commonly found in organisms, that is important for elimination unnecessary and damaged cells during development and adaptation to abiotic and biotic environmental stresses. PCD is a complex and precise, genetically controlled cellular process, in opposite to non-programmed death, necrosis, in which cells are "killed" by strong abiotic factors. This article shows: the occurrence of PCD during animals and plants ontogenesis, classification of cell death types in these organisms with description of autophagy, apoptosis and necrotic cell death and with discussion on plant cell death by apoptosis. The role of Bcl-2 protein and other proteins involved in the regulation of apoptosis induction and detection in the plant's (whose genomes do not encode these proteins) proteins of analogous function is also discussed. The paper also presents the effects of the expression of animals pro- and anti-apoptotic genes transformed into yeast and plants, and the use of transformed yeast as model to identify in cDNA libraries animal and plant genes involved in regulation of the induction and course of the PCD.

The reaction of Lupinus angustifolius L. root meristematic cell nucleoli to lead.

The effect of 2-48 h treatment of Lupinus angustifolius L. roots with lead nitrate at the concentration of 10(-4) M on the nucleoli in meristematic cells was investigated. In the lead presence the number of ring-shaped as well as segregated nucleoli increased especially after 12-48 h of treatment, while spindle-shaped nucleoli appeared after 24 h and 48 h. Lead presence also increased the frequency of cells with silver-stained particles in the nucleus and the number of these particles especially from the 12th hour of treatment. It was accompanied by significant decline of nucleolar area. Analysis of these cells in transmission electron microscope confirmed the presence of ring-shaped and segregated nucleoli. Moreover, electron microscopy revealed compact structure nucleoli without granular component. Additionally, one to three oval-shaped fibrillar structures attached to nucleolus or lying free in the nucleoplasm were visible. The possible mechanism of lead toxicity to the nucleolus is briefly discussed.

Proteins as nitrogen source for plants: a short story about exudation of proteases by plant roots.

Interest in the problem of plant nitrogen nutrition is increasing. Certain plants can use not only inorganic nitrogen, but also intact amino acids and short peptides. According to our studies, the roots of several agricultural and wild-living plants are able to exude proteases and by using them to create a pool of accessible N. This mini-review offers an overview of the problem of protease exudation by plant roots and its potential role in plant nitrogen nutrition.

Degradation of proteins by enzymes exuded by Allium porrum roots - a potentially important strategy for acquiring organic nitrogen by plants.

Nitrogen is one of the crucial elements that regulate plant growth and development. It is well-established that plants can acquire nitrogen from soil in the form of low-molecular-mass compounds, namely nitrate and ammonium, but also as amino acids. Nevertheless, nitrogen in the soil occurs mainly as proteins or proteins complexed with other organic compounds. Proteins are believed not to be available to plants. However, there is increasing evidence to suggest that plants can actively participate in proteolysis by exudation of proteases by roots and can obtain nitrogen from digested proteins. To gain insight into the process of organic nitrogen acquisition from proteins by leek roots (Allium porrum L. cv. Bartek), casein, bovine serum albumin and oxidized B-chain of insulin were used; their degradation products, after exposure to plant culture medium, were studied using liquid chromatography-mass spectrometry (LC-MS). Casein was degraded to a great extent, but the level of degradation of bovine serum albumin and the B-chain of insulin was lower. Proteases exuded by roots cleaved proteins, releasing low-molecular-mass peptides that can be taken up by roots. Various peptide fragments produced by digestion of the oxidized B-chain of insulin suggested that endopeptidase, but also exopeptidase activity was present. After identification, proteases were similar to cysteine protease from Arabidopsis thaliana. In conclusion, proteases exuded by roots may have great potential in the plant nitrogen nutrition.

The ability of plants to secrete proteases by roots.

The aim of our study was to find out if the culture medium of aseptically cultivated seedlings exhibits proteolytic activity and if this event is universal in angiospermous plants. Seedlings of 15 agricultural and wild-living plant species were cultivated for 14days without any addition of nutrients. Our studies showed that roots of higher plants could secrete proteases and that levels of proteolytic activity in the culture medium of individual species (and cultivars of the same species) could be significantly different. The differences between quantities of the secreted proteases were connected neither with the fresh weight of the growing seedlings nor with the surface of the root system. No proteins were required to induce secretion of proteases. The culture medium of a few studied species (Allium porrum, Zea mays, Helianthus annuus) showed the highest proteolytic activity at pH 7. Studies of the influence of standard protease inhibitors showed that examined proteases belong to the cysteine protease family. The results suggest that the apical parts of roots exuded proteases more intensively than mature parts. Our studies suggest that some plant species could develop a strategy to actively increase the level of free amino acids in the soil solution as a source of N. Our results may contribute to studying plant N nutrition in natural ecosystems and to increasing yield after organic fertilization of agricultural species.