Residues Clustered in the Light-Sensing Knot of Phytochrome B are Necessary for Conformer-Specific Binding to Signaling Partner PIF3 英文参考文献.docVIP

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Residues Clustered in the Light-Sensing Knot of Phytochrome B are Necessary for Conformer-Specific Binding to Signaling Partner PIF3 英文参考文献.doc

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Residues Clustered in the Light-Sensing Knot of Phytochrome B are Necessary for Conformer-Specific Binding to Signaling Partner PIF3 英文参考文献

ResiduesClusteredintheLight-SensingKnotof PhytochromeBareNecessaryforConformer-Specific BindingtoSignalingPartnerPIF3 EliseA.Kikis1,2.¤,YoshitoOka1,2.,MatthewE.Hudson3,AkiraNagatani4,PeterH.Quail1,2* 1DepartmentofPlantandMicrobialBiology,UniversityofCaliforniaBerkeley,Berkeley,California,UnitedStatesofAmerica,2USDA/ARS–PlantGeneExpressionCenter, Albany,California, United States of America, 3Department of CropSciences,University of Illinois, Urbana, Illinois, United States of America, 4Department of Biology, GraduateSchoolofScience,KyotoUniversity,Kyoto,Japan Abstract ThebHLHtranscriptionfactor,PHYTOCHROMEINTERACTINGFACTOR3(PIF3),interactsspecificallywiththephotoactivated, Pfr,formofArabidopsisphytochromeB(phyB).ThisinteractioninducesPIF3phosphorylationanddegradationinvivoand modulates phyB-mediated seedling deetiolation in response to red light. To identify missense mutations in the phyB N- terminal domain that disrupt this interaction, we developed a yeast reverse-hybrid screen. Fifteen individual mutations identified in this screen, or in previous genetic screens for Arabidopsis mutants showing reduced sensitivity to red light, wereshowntoalsodisruptlight-inducedbindingofphyBtoPIF3ininvitroco-immunoprecipitationassays.ThesephyB missensemutantsfallintotwogeneralclasses:ClassI(elevenmutants)containingthosedefectiveinlightsignalperception, duetoaberrantchromophoreattachmentorphotoconversion,andClassII(fourmutants)containingthosenormalinsignal perception,butdefectiveinthecapacitytotransducethissignaltoPIF3.Bygeneratingahomologymodelforthethree- dimensionalstructureoftheArabidopsisphyBchromophore-bindingregion,basedonthecrystalstructureofDeinococcus radioduransphytochrome,wepredictthatthreeofthefourClassIImutatedphyBresiduesaresolventexposedinacleft betweenthepresumptivePASandGAFdomains.Thisdeductionsuggeststhattheseresiduescouldbedirectlyrequiredfor thephysicalinteractionofphyBwithPIF3.BecausethesethreeresiduesarealsonecessaryforphyB-imposedinhibitionof hypocotylelo