Protein Phosphatase 2A Controls Ethylene Biosynthesis by Differentially Regulating the Turnover of ACC Synthase Isoforms 英文参考文献.docVIP

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Protein Phosphatase 2A Controls Ethylene Biosynthesis by Differentially Regulating the Turnover of ACC Synthase Isoforms 英文参考文献.doc

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Protein Phosphatase 2A Controls Ethylene Biosynthesis by Differentially Regulating the Turnover of ACC Synthase Isoforms 英文参考文献

ProteinPhosphatase2AControlsEthyleneBiosynthesis byDifferentiallyRegulatingtheTurnoverofACC SynthaseIsoforms KyleR.Skottke1,GyeongMeeYoon2,JosephJ.Kieber2,AlisonDeLong1* 1DepartmentofMolecularBiology,CellBiology,andBiochemistry,BrownUniversity,Providence,RhodeIsland,UnitedStatesofAmerica,2DepartmentofBiology,The UniversityofNorthCarolinaatChapelHill,ChapelHill,NorthCarolina,UnitedStatesofAmerica Abstract Thegaseoushormoneethyleneisoneofthemasterregulatorsofdevelopmentandphysiologythroughouttheplantlife cycle.Ethylenebiosynthesisisstringentlyregulatedtopermitmaintenanceoflowlevelsduringmostphasesofvegetative growthbuttoallowforrapidpeaksofhighproductionatdevelopmentaltransitionsandunderstressconditions.Inmost tissues ethylene is a negative regulator of cell expansion, thus low basal levels of ethylene biosynthesis in dark-grown seedlings are critical for optimal cell expansion during early seedling development. The committed steps in ethylene biosynthesisareperformedbytheenzymes1-aminocyclopropane1-carboxylatesynthase(ACS)and1-aminocyclopropane 1-carboxylateoxidase(ACO).TheabundanceofdifferentACSenzymesistightlyregulatedbothbytranscriptionalcontrol andbypost-translationalmodificationsandproteasome-mediateddegradation.HereweshowthatspecificACSisozymes aretargetsforregulationbyproteinphosphatase2A(PP2A)duringArabidopsisthalianaseedlinggrowthandthatreduced PP2A function causes increased ACS activity in the roots curl in 1-N-naphthylphthalamic acid 1 (rcn1) mutant. Genetic analysis reveals that ethylene overproduction in PP2A-deficient plants requires ACS2 and ACS6, genes that encode ACS proteinsknowntobestabilizedbyphosphorylation,andproteolyticturnoveroftheACS6proteinisretardedwhenPP2A activityisreduced.WefindthatPP2AandACS6proteinsassociateinseedlingsandthatRCN1-containingPP2Acomplexes specifically dephosphorylate a C-terminal ACS6 phosphopeptide. These results suggest that PP2A-dependent destabilization requires RCN1-dependent dephosphorylation of the ACS6 C-te