The vanadate-tolerant yeast Hansenula polymorpha undergoes cellular reorganization during growth in, and recovery from, the presence of vanadate.
When present at intracellular concentrations above micromolar, vanadate becomes toxic to most organisms. However, the yeast Hansenula polymorpha is able to grow on vanadate concentrations in the millimolar range, showing at the same time modifications in cellular ultrastructure and polyphosphate metabolism. Here, the development of the ultrastructural changes, and of vacuolar and secretory activities, during exponential growth on vanadate and upon a return to vanadate-free conditions was investigated. External invertase secretion was inhibited by vanadate, as shown by a decrease in external invertase activity, an intracellular accumulation of small vesicles and a cytoplasmic accumulation of internal invertase. An aberrant appearance of the cell wall and defects in cellular surface growth, possibly linked to defects in secretion, were also observed. However, inhibition of the secretory pathway was not complete since the activity of another secreted enzyme, exoglucanase, increased in the presence of vanadate. Growth on vanadate was also accompanied by an enhancement of vacuolar proteolysis, as indicated by an increase in carboxypeptidase Y activity. However, these modifications were all reversible upon return to vanadate-free conditions, with the normalization process being complex and involving new and dramatic ultrastructural changes and activation of an autophagic mechanism. This mechanism is involved in the elimination/resorption of the observed vanadate-induced aberrant cell structures and/or sites involved in vanadate accumulation, a necessary prerequisite for restoration of conventional ultrastructure and metabolic functions.
Dipartimento di Biotecnologie Agrarie ed Ambientali, Universit�di Ancona, Via Brecce Bianche, Ancona 60131,Italy.
Ilaria
I
Mannazzu
Dipartimento di Biotecnologie Agrarie ed Ambientali, Universit�di Ancona, Via Brecce Bianche, Ancona 60131,Italy.
Emanuela
E
Guerra
Dipartimento di Biotecnologie Agrarie ed Ambientali, Universit�di Ancona, Via Brecce Bianche, Ancona 60131,Italy.
Rosanna
R
Strabbioli
Dipartimento di Biotecnologie Agrarie ed Ambientali, Universit�di Ancona, Via Brecce Bianche, Ancona 60131,Italy.
Dario
D
Pediconi
Dipartimento di Biotecnologie Agrarie ed Ambientali, Universit�di Ancona, Via Brecce Bianche, Ancona 60131,Italy.
Fabrizio
F
Fatichenti
D002268:Carboxypeptidases / Q000378:metabolism; D043402:Cathepsin A; D002473:Cell Wall / Q000187:drug effects / Q000648:ultrastructure; D003593:Cytoplasm / Q000187:drug effects / Q000648:ultrastructure; D006026:Glycoside Hydrolases / Q000378:metabolism; D008854:Microscopy, Electron; D010843:Pichia / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure*; D011122:Polyphosphates / Q000378:metabolism; D014617:Vacuoles / Q000187:drug effects / Q000648:ultrastructure; D014638:Vanadates / Q000494:pharmacology*; D043324:beta-Fructofuranosidase
D011122:Polyphosphates; D014638:Vanadates; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase; D002268:Carboxypeptidases; D043402:Cathepsin A