Abstract
The PPX1 and PPN1 genes of Saccharomyces cerevisiae encode the enzymes that hydrolyze inorganic polyphosphates (polyP) of different chain lengths including tripolyphosphate. They are divalent metal ion dependent. PPX1 is an exopolyphosphatase splitting Pi from polyP chain end. PPN1 displays exopolyphosphatase and endopolyphosphatase activities in the presence of cobalt and magnesium ions, respectively. PPN1 prefers long-chain polyP, while PPX1 prefers short-chain polyP. Commonly, PPX1 is localized in the cytoplasm and mitochondrial matrix, while PPN1 is localized in the vacuoles, nuclei, and mitochondrial membrane. PPN1 appears in the cytoplasm at the early growth stage under phosphate excess. The PPX1 or PPN1 knockouts increase polyP content in S. cerevisiae. ΔPPN1 mutants contain polyP with longer chains, while ΔPPX1 does not demonstrate polyP chain elongation. PPX1 overexpression has no effect on polyP content and chain length. In turn, PPN1 overexpression decreases polyP content. Both PPX1 and PPN1 catalyze the same reaction, but there is no similarity between the amino acid sequences of these enzymes. Furthermore, the human ortholog of PPX1, the prune protein, has an exopolyphosphatase activity, but neither functional nor structural homologs of PPN1 have been found in higher eukaryotes.
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The authors were supported by the Russian Foundation for Basic Research (grant 14-04-00515).
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Andreeva, N., Lichko, L., Trilisenko, L., Kulakovskiy, I.V., Kulakovskaya, T. (2016). Yeast Polyphosphatases PPX1 and PPN1: Properties, Functions, and Localization. In: Kulakovskaya, T., Pavlov, E., Dedkova, E. (eds) Inorganic Polyphosphates in Eukaryotic Cells. Springer, Cham. https://doi.org/10.1007/978-3-319-41073-9_2
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