Inactivation of endopolyphosphatase gene PPN1 results in inhibition of expression of exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase not encoded by PPX1 in Saccharomyces cerevisiae

• Published in: Biochimica et biophysica acta Vol. 1674; no. 1; pp. 98 - 102
• Main Authors: Lichko, Lidiya, Kulakovskaya, Tatyana, Kulaev, Igor
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 06.09.2004
• Subjects: Acid Anhydride Hydrolases - chemistry; Acid Anhydride Hydrolases - genetics; Acid Anhydride Hydrolases - metabolism; Cell Size; Cytosol; Exopolyphosphatase; Gene Expression Regulation, Fungal; Gene Silencing; Molecular Weight; Phenotype; Polyphosphate; PPX1 and PPN1 mutants; Saccharomyces cerevisiae; Saccharomyces cerevisiae - cytology; Saccharomyces cerevisiae - enzymology; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; PPX1 and PPN1 mutants; Exopolyphosphatase; Polyphosphate; Cytosol; Saccharomyces cerevisiae
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2004.06.004

Saccharomyces cerevisiae possesses multiple forms of exopolyphosphatases, the enzymes involved in the metabolism of inorganic polyphosphates, which are important regulatory compounds. In S. cerevisiae, inactivation of endopolyphosphatase gene PPN1 leads to the inhibition of expression of both exopolyphosphatase PPX1 and high-molecular-mass exopolyphosphatase of ∼1000 kDa not encoded by PPX1. In the single endopolyphosphatase mutant CRN, the expression of exopolyphosphatase PPX1 decreases 6.5-fold and 2.5-fold at the stationary and exponential growth phases, respectively, as compared with the parent strain CRY. In this mutant, the activity of the high-molecular-mass exopolyphosphatase of ∼1000 kDa decreases ∼10-fold as compared with that in strains with the PPN1 gene. In a double mutant of PPX1 and PPN1, no exopolyphosphatase activity is detected in the cytosol at the stationary growth phase. Thus, the exopolyPase activity in cell cytosol depends on the endopolyPase gene PPN1.