1999
Modulation of GT-1 DNA-binding activity by calcium-dependent phosphorylation
Maréchal E, Hiratsuka K, Delgado J, Nairn A, Qin J, Chait B, Chua N. Modulation of GT-1 DNA-binding activity by calcium-dependent phosphorylation. Plant Molecular Biology 1999, 40: 373-386. PMID: 10437822, DOI: 10.1023/a:1006131330930.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsArabidopsisBase SequenceBinding SitesCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesDNA PrimersDNA-Binding ProteinsIn Vitro TechniquesMolecular Sequence DataNuclear ProteinsPhosphorylationPlants, ToxicRatsRecombinant ProteinsSequence Homology, Amino AcidSubstrate SpecificityTranscription FactorsConceptsDNA-binding activityCalcium-dependent phosphorylationGene expressionMolecular switchGT-1Analysis of mutantsDNA-binding proteinsLight-grown plantsPost-translational modificationsCalf intestine phosphataseCalcium/calmodulin kinasePhosphorylatable residuesCasein kinaseGene activationMass spectrometry analysisPromoter sequencesDNA bindingKinase activityBoxIICalmodulin kinasePhosphorylationHGT-1Novo synthesisDephosphorylationSpectrometry analysis
1998
Isolation and Characterization of PNUTS, a Putative Protein Phosphatase 1 Nuclear Targeting Subunit*
Allen P, Kwon Y, Nairn A, Greengard P. Isolation and Characterization of PNUTS, a Putative Protein Phosphatase 1 Nuclear Targeting Subunit*. Journal Of Biological Chemistry 1998, 273: 4089-4095. PMID: 9461602, DOI: 10.1074/jbc.273.7.4089.Peer-Reviewed Original ResearchConceptsPhosphatase 1 nuclear targeting subunitProtein phosphatase 1Targeting subunitPP1 catalytic activityMammalian cell lysatesTwo-hybrid assayPP1 functionsNuclear functionsNuclear compartmentalizationNovel proteinPhosphatase 1Subcellular localizationCell physiologyCell lysatesCell nucleiSubunitsExogenous substratesInitial characterizationProteinStable complexesPotent modulationChromatinCloningMitosisCompartmentalization
1995
Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
Goldberg J, Huang H, Kwon Y, Greengard P, Nairn A, Kuriyan J. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature 1995, 376: 745-753. PMID: 7651533, DOI: 10.1038/376745a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCatalysisCrystallography, X-RayDopamine and cAMP-Regulated Phosphoprotein 32Escherichia coliHumansIntracellular Signaling Peptides and ProteinsMetalsMicrocystinsModels, MolecularMolecular Sequence DataNerve Tissue ProteinsNuclear ProteinsPeptides, CyclicPhosphoprotein PhosphatasesPhosphoproteinsProtein ConformationProtein Phosphatase 1ProteinsRabbitsRecombinant ProteinsRNA-Binding ProteinsSequence Homology, Amino AcidConceptsPhosphatase 1Protein serine/threonine phosphatase-1Serine/threonine phosphatase 1Mammalian protein phosphatase 1Protein phosphatase 1Potential binding sitesThree-dimensional structureCatalytic subunitRegulatory sequencesCatalytic domainCarboxy terminusΒ scaffoldBinding sitesActive siteSurface groovesTerminusSubunitsDomainProteinCrystal structureSitesTyrosineMetalloenzymesSequenceToxin