Effect of PPX1 inactivation on exopolyphosphatases of different cell compartments of the yeast Saccharomyces cerevisiae.
Inactivation of PPX1 encoding a major exopolyphosphatase (PPX1) in Saccharomyces cerevisiae results in a change of exopolyphosphatase spectra in the yeast cells. In the PPX1-deficient strain, an elimination of approximately 45 kDa enzyme is observed in cytosol and cell envelopes, and the activity of an exopolyphosphatase with a molecular mass of approximately 830 kDa increases 5-fold in the cytosol. These two enzyme activities differ greatly from each other not only in molecular masses but also in biochemical properties. Inactivation of PPX1 does not result in any changes in the content and properties of vacuolar exopolyphosphatase as compared with the wild strain of S. cerevisiae. In response to PPX1 mutation, exopolyphosphatase properties in the cell as a whole undergo modifications including the ability to hydrolyze polyphosphates with different lengths of the chain.
Lichko
Lidia
L
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russia. alla@ibpm.serpukhov.su
Kulakovskaya
Tatyana
T
Kulaev
Igor
I
D017766:Acid Anhydride Hydrolases / Q000378:metabolism*; D002451:Cell Compartmentation; D002462:Cell Membrane / Q000201:enzymology; D003600:Cytosol / Q000201:enzymology; D004789:Enzyme Activation; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D014617:Vacuoles / Q000201:enzymology
D017766:Acid Anhydride Hydrolases; C020137:exopolyphosphatase