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Difference between revisions of "Aguilaniu 2001 J Biol Chem"

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{{Labeling
|instruments=Oxygraph-2k
|instruments=Oxygraph-2k
|injuries=Aging; Senescence
|organism=Yeast; Fungi
|organism=Yeast; Fungi
|topics=Respiration; OXPHOS; ETS Capacity
|topics=Respiration; OXPHOS; ETS Capacity
|discipline=Mitochondrial Physiology
|discipline=Mitochondrial Physiology
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Revision as of 11:55, 17 November 2011

Publications in the MiPMap
Aguilaniu H, Gustafsson L, Rigoulet M, Nystrom T (2001) Protein oxidation in G0 cells of Saccharomyces cerevisiae depends on the state rather than rate of respiration and is enhanced in pos9 but not yap1 mutants. J. Biol. Chem. 276: 35396-35404.

Β» PMID: 11431467

Aguilaniu H, Gustafsson L, Rigoulet M, Nystrom T (2001) J. Biol. Chem.

Abstract: Immunodetection of protein carbonyl groups demonstrates that growth arrest elicited by carbon or nitrogen starvation causes an increased oxidation of proteins in Saccharomyces cerevisiae. Mutant analysis suggests that the response regulator Pos9p is involved in mitigating self-inflicted oxidative damages in G0 cells, whereas Yap1p is primarily required in growing cells. The data also suggest that oxidation of target proteins is not a priori an effect of arrest of cell division or nutrient depletion and cannot be explained by the respiratory activity alone nor a high ratio of catabolic/anabolic activity in G0 cells. Instead, we observed that starvation elicits a transition in the respiratory state (from phosphorylating to nonphosphorylating respiration) and that this transition is associated with a stepwise increase in protein oxidation. During carbon starvation, this transition and increase in oxidation occurs immediately as the carbon source is depleted, growth is arrested, and the respiratory rate falls drastically. In contrast, during nitrogen starvation and excess carbon the respiratory state transition and stepwise increase in protein oxidation are markedly delayed and occur long after the nitrogen source has been depleted and division and growth-arrested. Oxidation in G0 cells could be enhanced by treating cells with low concentrations of antimycin A and attenuated with myxothiazol, indicating that protein oxidation is intimately linked to reactive oxygen species generated by semiquinones of the Q-cycle. Thus, the work presented suggests that the degree of coupling in the mitochondrial respiratory apparatus rather then the overall rate of respiration affects the degree of protein oxidation in nondividing yeast cells.


β€’ O2k-Network Lab: FR_Bordeaux_Rigoulet M


Labels:

Stress:Aging; Senescence"Aging; Senescence" is not in the list (Cell death, Cryopreservation, Ischemia-reperfusion, Permeability transition, Oxidative stress;RONS, Temperature, Hypoxia, Mitochondrial disease) of allowed values for the "Stress" property.  Organism: Yeast; Fungi"Yeast; Fungi" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property. 


Regulation: Respiration; OXPHOS; ETS Capacity"Respiration; OXPHOS; ETS Capacity" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property. 


HRR: Oxygraph-2k