In vivo activation of the yeast plasma membrane ATPase during nitrogen starvation. Identification of the regulatory domain that controls activation.
Yeast plasma membrane ATPase is activated during nitrogen starvation when a fermentable substrate is present. This activation is due to changes in the Vmax and it is irreversible, independent of protein synthesis and apparently triggered by a decrease in the intracellular pH. It is shown that the ATPase regulatory domain implicated in the activation by fermentable carbon sources is also implicated in activation by nitrogen starvation and by external acidification.
Benito
B
B
Instituto de Investigaciones Biomédicas del CSIC, Madrid, Spain.
Portillo
F
F
Lagunas
R
R
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D002462:Cell Membrane / Q000201:enzymology; D004789:Enzyme Activation / Q000502:physiology; D005285:Fermentation; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D009584:Nitrogen / Q000378:metabolism* / Q000502:physiology; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity
D005656:Fungal Proteins; D008565:Membrane Proteins; D000251:Adenosine Triphosphatases; D009584:Nitrogen