Tags

Type your tag names separated by a space and hit enter

Inorganic polyphosphates and exopolyphosphatases in cell compartments of the yeast Saccharomyces cerevisiae under inactivation of PPX1 and PPN1 genes.
Biosci Rep. 2006 Feb; 26(1):45-54.BR

Abstract

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.

Authors+Show Affiliations

Lichko L
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia. alla@ibpm.pushchino.ru
Kulakovskaya T
No affiliation info available
Pestov N
No affiliation info available
Kulaev I
No affiliation info available

MeSH

Acid Anhydride HydrolasesCell CompartmentationGene SilencingGenes, FungalPolyphosphatesSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16779667

Citation

Lichko, Lidiya, et al. "Inorganic Polyphosphates and Exopolyphosphatases in Cell Compartments of the Yeast Saccharomyces Cerevisiae Under Inactivation of PPX1 and PPN1 Genes." Bioscience Reports, vol. 26, no. 1, 2006, pp. 45-54.
Lichko L, Kulakovskaya T, Pestov N, et al. Inorganic polyphosphates and exopolyphosphatases in cell compartments of the yeast Saccharomyces cerevisiae under inactivation of PPX1 and PPN1 genes. Biosci Rep. 2006;26(1):45-54.
Lichko, L., Kulakovskaya, T., Pestov, N., & Kulaev, I. (2006). Inorganic polyphosphates and exopolyphosphatases in cell compartments of the yeast Saccharomyces cerevisiae under inactivation of PPX1 and PPN1 genes. Bioscience Reports, 26(1), 45-54.
Lichko L, et al. Inorganic Polyphosphates and Exopolyphosphatases in Cell Compartments of the Yeast Saccharomyces Cerevisiae Under Inactivation of PPX1 and PPN1 Genes. Biosci Rep. 2006;26(1):45-54. PubMed PMID: 16779667.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Inorganic polyphosphates and exopolyphosphatases in cell compartments of the yeast Saccharomyces cerevisiae under inactivation of PPX1 and PPN1 genes. AU - Lichko,Lidiya, AU - Kulakovskaya,Tatyana, AU - Pestov,Nikolai, AU - Kulaev,Igor, PY - 2006/6/17/pubmed PY - 2006/8/11/medline PY - 2006/6/17/entrez SP - 45 EP - 54 JF - Bioscience reports JO - Biosci Rep VL - 26 IS - 1 N2 - 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. SN - 0144-8463 UR - https://www.unboundmedicine.com/medline/citation/16779667/Inorganic_polyphosphates_and_exopolyphosphatases_in_cell_compartments_of_the_yeast_Saccharomyces_cerevisiae_under_inactivation_of_PPX1_and_PPN1_genes_ DB - PRIME DP - Unbound Medicine ER -
Grapherence [↓13]

Related Citations

More