Plant cell elongation growth is an integral process involved in different plant movements (tropisms); it provides the possibility to reach different resources of energy, water and nutrition and is therefore important for metabolism and development. Cell multiple enlargement along the longitudinal axis is commonly accepted to be under the control of the phytohormone auxin. One of the key enzymes involved in elongation is the plasma membrane H + -ATPase, which is known to acidify the cell wall. Investigation of the role of the proton pump at the plasma membrane was initiated by Prof. Vsevolod V. Polevoi and still is in progress in the group of Prof. Maria F. Shishova at the Department of Plant Physiology and Biochemistry, St. Petersburg State University. Different mechanisms of post-translation regulation of H + -pump activity are discussed in this review. We also suggest a possible scheme of elongation growth based on the shift in plant cell sensitivity to auxin and on its facility to elongate.

The tonoplast is an intracellular membrane, important for numerous functions of the vacuoles in plant cells. Transport, signaling, enzymatic activity and other processes of the tonoplast are the focus of a wide spectrum of studies. Multiple advanced analyses demand highly purified vacuoles or vesicles of the tonoplast membrane fraction. Since 1960 several approaches have been developed for such purification, but new goals and new model objects require adjustment of already existing techniques. The presented investigation aimed to compare two methods of tonoplast membrane fraction purification from tobacco suspension cell culture BY-2 (Nicotiana tabacum L., cv Bright Yellow) based on sucrose and sucrose/sorbitol gradients. The functional activity of obtained purified tonoplast fractions was measured by the hydrolytic activity of vacuolar H+-ATPase and H+-PPase.

Вакуолярная Н + -АТФаза является одним из наиболее важных и широко распространенных протон-транспортирующих ферментов эукариотической клетки. Она выполняет жизненно важные функции и представляет собой мультисубъединичный комплекс, состоящий из двух функциональных доменов V 1 и V 0 . В представленном обзоре рассматриваются современные представления о многоуровневой регуляции V-АТФазы растительного организма. Целый ряд субъединиц кодируется более чем одним геном. В связи с этим рассматривается значение регуляции на транскрипционном уровне. Особое внимание уделено рассмотрению многочисленных способов регуляции работы фермента на посттрансляционном уровне. Библиогр. 60 назв. Табл. 1. PECULIAR FEATURES OF PLANT CELL VACUOLAR H + -ATPASE REGULATIONSt. Petersburg State University, 7-9, Universitetskaya nab., St. Petersburg, 199034, Russian Federation; nastin1972@mail.ru, ctz1985@mail.ru, daria-rom@yandex.ru, bootika@mail.ru, mshishova@mail.ru Vacuolar Н + -АТPase is one of the most crucial and widely spread proton-transporting enzymes of eukaryotic cells. It fulfi ls many vital functions. Th e enzyme is represented as a multisubunit complex, organized in two domains, V 1 and V 0 . Th e review summarizes modern data on plant cell H + -V-ATPase. Regulation of proton pump activity is analyzed for diff erent level of plant organism complicity. A number of vacuolar Н + -АТPase subunits are encoded by more than one gene. Th us the importance of regulation at transcription level is discussed. Special attention is paid to analysis of diff erent ways of regulating activity of the enzyme at post-translation level. Refs 60. Table 1.

Vacuolar H+-ATPase is a multi-subunit protein complex, which fulfills a number of crucial functions in plant cell. Different mechanisms are known to be important for the regulation of proton-transporting enzyme activity at transcriptional and post-translational levels. In this investigation we performed a comparison analysis of molecular phylogeny of different subunits of vacuolar H+-ATPase directed in the elucidation of conservative rate of membrane and peripheral complexes of the enzyme. High rate of conservatism was shown for subunits c, d and В, as well as ancient duplications of subunit a.