The RNA editing is one of the post-transcriptional modifications which prepare RNA for fulfilling its function. It is well known that editing is a common process for most of eukaryotic organisms (from protozoan to human) and for some groups of viruses, however its mechanism is specific for species, genera and kingdoms. Up to now RNA editing is well characterized for few species only. It is suggested that substitutional RNA editing is conducted by deaminase so as it does not lead to the sugar-phosphate backbone brakeage.

Chloroplasts of higher plants contain thylakoid membranes differentiated into several cylindri- cal granum stacks of appressed (stacked) membrane which are surrounded by non-appressed (unstacked) helically organized stroma thylakoids. The light reactions of photosynthesis are mediated by chlorophyll- protein complexes – Photosystem I (PSI) and Photosystem II (PSII) differentially embedded in granum and stroma membranes. Moreover, electron transport and conversion of light energy into ATP depend on cytochromes b6f and ATP synthase complexes.

Dynamin and dynamin-related proteins (DRP) participate in many processes essential for normal function of the cells and organisms. They were found both in animals and plants. In Arabidopsis thaliana 16 different dynamin-related proteins were identified that are grouped into six subfamilies. DRP1 and soybean fragmoplastin participate in the cell plate formation during cytokinesis. Two mem- bers of DRP2 subfamily display domain structure similar to mammalian classical dynamins and may be involved in endocytosis and membrane recycling via clathrin-coated vesicles.

Dynamin and dynamin-related proteins (DRP) participate in many processes essential for normal function of the cells and organisms. They were found both in animals and plants. In Arabidopsis thaliana 16 different dynamin-related proteins were identified that are grouped into six subfamilies. DRP1 and soybean fragmoplastin participate in the cell plate formation during cytokinesis. Two mem- bers of DRP2 subfamily display domain structure similar to mammalian classical dynamins and may be involved in endocytosis and membrane recycling via clathrin-coated vesicles.