Role of the GYVG Pore Motif of HslU ATPase in Protein Unfolding and Translocation for Degradation by HslV Peptidase*
Park E, Rho YM, Koh OJ, Ahn SW, Seong IS, Song JJ, Bang O, Seol JH, Wang J, Eom SH, Chung CH. Role of the GYVG Pore Motif of HslU ATPase in Protein Unfolding and Translocation for Degradation by HslV Peptidase*. Journal Of Biological Chemistry 2005, 280: 22892-22898. PMID: 15849200, DOI: 10.1074/jbc.m500035200.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid MotifsAmino Acid SequenceCaseinsChromatographyCross-Linking ReagentsDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEndopeptidase ClpEscherichia coliEscherichia coli ProteinsGlycineHydrolysisModels, BiologicalModels, MolecularMolecular Sequence DataMutagenesisMutagenesis, Site-DirectedMutationPeptidesProtein BindingProtein DenaturationProtein FoldingProtein TransportSequence Homology, Amino AcidTemperatureConceptsHslU ATPasePore motifHslVU complexHslV peptidaseCentral poreATP-dependent proteaseProtein unfoldingProteolytic active sitesHslU hexamerProteolytic chamberHslV dodecamerUnfolded proteinsHslV.HslUGly residueTranslocation processAmino acidsDegradation of caseinMotifProteinATP cleavageSame structural featuresATPase activityTranslocationATPase