Point mutations in the different domains of the plasma membrane PMA1 ATPase cause redistribution among fractions of inorganic polyphosphates.

Both ATP and inorganic polyphosphates (PolyP) appeared to be involved in the yeast energy homeostasis, in which plasma membrane PMA1 H-АТРase plays one of the key roles. During biogenesis and functioning, the enzyme undergoes structural and regulatory phosphorylation. Aim of the work was to elucidate interconnection between functioning of the yeast PMA1 H-АТРase carrying point substitutions that affected the enzyme structure-function relationship and its ability to be phosphorylated and PolyP metabolism.