Extracellular Glucose Increases the Coupling Capacity of the Yeast V H+-ATPase and the Resistance of Its H+ Transport Activity to Nitrate Inhibition 英文参考文献.docVIP

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Extracellular Glucose Increases the Coupling Capacity of the Yeast V H+-ATPase and the Resistance of Its H+ Transport Activity to Nitrate Inhibition 英文参考文献.doc

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ExtracellularGlucoseIncreasestheCouplingCapacityoftheYeastVH-ATPaseandtheResistanceofItsHTransportActivitytoNitrateInhibition英文参考文献

ExtracellularGlucoseIncreasestheCouplingCapacityof theYeastVH -ATPaseandtheResistanceofItsH TransportActivitytoNitrateInhibition + + CamilaC.Ribeiro1,2.,RenanM.Monteiro1.,FlaviaP.Freitas1.,ClaudioRetamal2.,LayzR.S.Teixeira1, LiviaM.Palma1,FlaviaE.Silva1,ArnoldoR.Fac?anha2,AnnaL.Okorokova-Fac?anha1,LevA.Okorokov1* 1Laborato′riodeFisiologiaeBioqu?′micadeMicrorganismos,CentrodeBiocie?nciaeBiotecnologia,UniversidadeEstadualdoNorteFluminenseDarcyRibeiro,Camposdos Goytacazes,Brasil,2Laborato′riodeBiologiaCelulareTecidual,CentrodeBiocie?nciaeBiotecnologia,UniversidadeEstadualdoNorteFluminenseDarcyRibeiro,Campos dosGoytacazes,Brasil Abstract V H+-ATPase has an important role in a variety of key physiological processes. This enzyme is reversibly activated/partly inactivatedbytheaddition/exhaustionofextracellularglucose.Thecurrentmodelofitsregulationassumesthereversible disassembly/reassemblyof,60–70%oftheV1andV0membranecomplexes,whichareresponsibleforATPhydrolysisand + H conductance,respectively.Thenumberofassembledcomplexesdeterminesthepumpactivitybecausedisassembled complexes are inactive. The model predicts the identical catalytic properties for the activated and semi-active enzymes molecules. To verify the model predictions we have isolated total membranes from yeast spheroplasts that were pre- incubatedeitherwithorwithoutglucose.NitratetreatmentofmembranesrevealedthesimilarATPaseinhibitionfortwo + enzymestates,suggestingthattheyhaveidenticalstructuresthatareessentialforATPhydrolysis.However,H transport wasinhibitedmorethantheATPaseactivities,indicatinganitrateuncouplingaction,whichwassignificantlyhigherforthe nonactivated enzyme. This finding suggests that the structure of the non-activated enzyme, which is essential for H+ transport, is lessstable thanthat of theactivated enzyme. Moreover, theglucose activation ofthe pump increases i )its + + couplingcapacity;ii)itsKMforATPhydrolysisandATPaffinityforH transport;iii)theVmaxforH transportincomparison w