Purification and properties of polyphosphatase fromSaccharomyces cerevisiae cytosol

Andreeva, N. A.; Kulakovskaya, T. V.; Sidorov, Igor A.; Karpov, A. V.; Kulaev, I. S.

doi:10.1002/(sici)1097-0061(19980315)14:4<383::aid-yea232>3.0.co;2-s

Cited by 13 publications

References 15 publications

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Enzymes of Inorganic Polyphosphate Metabolism

Kulakovskaya

Kulaev

2013

Progress in Molecular and Subcellular Biology

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Inorganic polyphosphate (PolyP) is a linear polymer containing a few to several hundred orthophosphate residues linked by energy-rich phosphoanhydride bonds. Investigation of PolyP-metabolizing enzymes is important for medicine, because PolyPs perform numerous functions in the cells. In human organism, PolyPs are involved in the regulation of Ca(2+) uptake in mitochondria, bone tissue development, and blood coagulation. The essentiality of polyphosphate kinases in the virulence of pathogenic bacteria is a basis for the discovery of new antibiotics. The properties of the major enzymes of PolyP metabolism, first of all polyphosphate kinases and exopolyphosphatases, are described in the review. The main differences between the enzymes of PolyP biosynthesis and utilization of prokaryotic and eukaryotic cells, as well as the multiple functions of some enzymes of PolyP metabolism, are considered.

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Enzymes of Inorganic Polyphosphate Metabolism

Kulakovskaya

Kulaev

2013

Progress in Molecular and Subcellular Biology

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Inorganic Polyphosphate: A Molecule of Many Functions

Kornberg

1999

Progress in Molecular and Subcellular Biology

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Inorganic Polyphosphates and Exopolyphosphatases in Cell Compartments of the Yeast Saccharomyces cerevisiae Under Inactivation of PPX1 and PPN1 Genes

et al. 2006

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Purified fractions of cytosol, vacuoles, nuclei, and mitochondria of Saccharomyces cerevisiae possessed inorganic polyphosphates with chain lengths characteristic of each individual compartment. The most part (80-90%) of the total polyphosphate level was found in the cytosol fractions. Inactivation of a PPX1 gene encoding ~40-kDa exopolyphosphatase substantially decreased exopolyphosphatase activities only in the cytosol and soluble mitochondrial fraction, the compartments where PPX1 activity was localized. This inactivation slightly increased the levels of polyphosphates in the cytosol and vacuoles and had no effect on polyphosphate chain lengths in all compartments. Exopolyphosphatase activities in all yeast compartments under study critically depended on the PPN1 gene encoding an endopolyphosphatase. In the single PPN1 mutant, a considerable decrease of exopolyphosphatase activity was observed in all the compartments under study. Inactivation of PPN1 decreased the polyphosphate level in the cytosol 1.4-fold and increased it 2- and 2.5-fold in mitochondria and vacuoles, respectively. This inactivation was accompanied by polyphosphate chain elongation. In nuclei, this mutation had no effect on polyphosphate level and chain length as compared with the parent strain CRY. In the double mutant of PPX1 and PPN1, no exopolyphosphatase activity was detected in the cytosol, nuclei, and mitochondria and further elongation of polyphosphates was observed in all compartments.

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Purification and properties of polyphosphatase fromSaccharomyces cerevisiae cytosol

Cited by 13 publications

References 15 publications

Enzymes of Inorganic Polyphosphate Metabolism

Enzymes of Inorganic Polyphosphate Metabolism

Inorganic Polyphosphate: A Molecule of Many Functions

Inorganic Polyphosphates and Exopolyphosphatases in Cell Compartments of the Yeast Saccharomyces cerevisiae Under Inactivation of PPX1 and PPN1 Genes

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