2020
Chaperonin-assisted protein folding: a chronologue
Horwich AL, Fenton WA. Chaperonin-assisted protein folding: a chronologue. Quarterly Reviews Of Biophysics 2020, 53: e4. PMID: 32070442, DOI: 10.1017/s0033583519000143.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino AcidsAnimalsCarbon DioxideChaperoninsCytosolDimerizationHeat-Shock ProteinsHumansHydrophobic and Hydrophilic InteractionsKineticsMiceMitochondriaMutationNeurosporaProtein ConformationProtein DenaturationProtein FoldingRibonuclease, PancreaticRibulose-Bisphosphate CarboxylaseSurface PropertiesTemperature
2001
Folding of malate dehydrogenase inside the GroEL–GroES cavity
Chen J, Walter S, Horwich A, Smith D. Folding of malate dehydrogenase inside the GroEL–GroES cavity. Nature Structural & Molecular Biology 2001, 8: 721-728. PMID: 11473265, DOI: 10.1038/90443.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBinding SitesChaperonin 10Chaperonin 60Chromatography, High Pressure LiquidDeuteriumDimerizationHydrogen BondingKineticsMalate DehydrogenaseMass SpectrometryMitochondria, HeartModels, MolecularPeptide FragmentsProtein BindingProtein DenaturationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsSwineConceptsMalate dehydrogenaseNonnative substrate proteinGroEL-GroES cavitySubstrate proteinsProductive foldingChaperonin GroELApical domainGroESGroELMechanical unfoldingGlobal destabilizationSecondary structureHydrophilic chamberCentral cavityInitial proteinDeuterium exchangeFoldingProteinATPDehydrogenaseHydrophobic central cavityMass spectrometryOpen ringPolypeptideUnfoldingClpA mediates directional translocation of substrate proteins into the ClpP protease
Reid B, Fenton W, Horwich A, Weber-Ban E. ClpA mediates directional translocation of substrate proteins into the ClpP protease. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 3768-3772. PMID: 11259663, PMCID: PMC31127, DOI: 10.1073/pnas.071043698.Peer-Reviewed Original ResearchConceptsSubstrate proteinsClpP proteaseUnfolded substrate proteinsATP-dependent unfoldingATP-dependent mannerATP-dependent translocationChaperone ClpAProteolytic chamberFluorescence resonance energy transferDirectional translocationCOOH terminusClpAResonance energy transferProteinTranslocationIntracellular degradationFluorescence anisotropyProteaseRing complexTerminusLarge assembliesDonor fluorophoreRecognition elementRecent studiesHslUVMechanisms of protein folding
Grantcharova V, Alm E, Baker D, Horwich A. Mechanisms of protein folding. Current Opinion In Structural Biology 2001, 11: 70-82. PMID: 11179895, DOI: 10.1016/s0959-440x(00)00176-7.Peer-Reviewed Original ResearchConceptsEscherichia coli chaperonin GroELNon-native proteinsATP-dependent formationCo-chaperonin GroESLowest free energy pathChaperonin GroELProtein foldingUnfolded proteinsLarge proteinsGroELNative stateNative structureContact orderProteinChaperoninKinetic trapsFoldingChaperonesGroESFree energy pathPolypeptideComplexes
1997
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL
Goldberg M, Zhang J, Sondek S, Matthews C, Fox R, Horwich A. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 1080-1085. PMID: 9037009, PMCID: PMC19747, DOI: 10.1073/pnas.94.4.1080.Peer-Reviewed Original ResearchConceptsNative-like structureChaperonin GroELDihydrofolate reductaseProtein-folding intermediatesNative dihydrofolate reductaseStopped-flow fluorescence experimentsNonnative proteinsSubstrate proteinsProductive foldingPresence of ATPHuman dihydrofolate reductaseHydrogen-deuterium exchangeGroELPrimary structureProteinCentral channelHydrophobic interactionsFluorescence experimentsGroESFoldingSpeciesReductaseNMR spectroscopyDistant partsATP
1996
Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction
Weissman J, Rye H, Fenton W, Beechem J, Horwich A. Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction. Cell 1996, 84: 481-490. PMID: 8608602, DOI: 10.1016/s0092-8674(00)81293-3.Peer-Reviewed Original ResearchConceptsCis ternary complexProtein foldingRelease of GroESAddition of GroESFolding reactionTernary complexNonhydrolyzable ATP analogGroES releaseProtein folding reactionSubstrate proteinsPresence of ATPGroEL mutantGroEL-GroESGroEL complexNonnative substratesATP hydrolysisGroESComplete foldingSubstrate flexibilityATP analogFoldingFluorescence anisotropyActive stateATPRecent studies
1994
GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
Weissman J, Kashi Y, Fenton W, Horwich A. GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell 1994, 78: 693-702. PMID: 7915201, DOI: 10.1016/0092-8674(94)90533-9.Peer-Reviewed Original ResearchConceptsCochaperonin GroESMultiple roundsGroEL functionChaperonin GroELKinetic partitioningMutant formsNonnative conformationsNonnative formsGroELAddition of ATPGroEL moleculeTryptophan fluorescenceFolding reactionDouble-ring structureUnfolded statePolypeptideDiverse setGroESProteolysisProteinATPBindingFateConformationComplexes
1992
TCP1 complex is a molecular chaperone in tubulin biogenesis
Yaffe M, Farr G, Miklos D, Horwich A, Sternlicht M, Sternlicht H. TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature 1992, 358: 245-248. PMID: 1630491, DOI: 10.1038/358245a0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCycloheximideDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsKineticsMacromolecular SubstancesMicrotubule-Associated ProteinsMolecular WeightNuclear ProteinsProtein BiosynthesisProtein ConformationRabbitsReticulocytesRNA, MessengerT-Complex Genome RegionTubulinUbiquitin-Protein LigasesConceptsReticulocyte lysateTubulin subunitsCytosol of eukaryotesComplex polypeptide 1Protease-sensitive conformationRabbit reticulocyte lysateCytosolic chaperonesTubulin biogenesisMajor cytosolic proteinMolecular chaperonesTCP1 complexK proteinCytosolic proteinsΒ heterodimerBiogenesisPolypeptide 1Β-tubulinProteinSubunitsChaperonesMg-ATPK-complexesMolecular targetsNonhydrolysable analogueTubulin
1991
Protein folding causes an arrest of preprotein translocation into mitochondria in vivo.
Wienhues U, Becker K, Schleyer M, Guiard B, Tropschug M, Horwich A, Pfanner N, Neupert W. Protein folding causes an arrest of preprotein translocation into mitochondria in vivo. Journal Of Cell Biology 1991, 115: 1601-1609. PMID: 1757464, PMCID: PMC2289212, DOI: 10.1083/jcb.115.6.1601.Peer-Reviewed Original ResearchMeSH KeywordsAminopterinBiological TransportIntracellular MembranesKineticsL-Lactate DehydrogenaseL-Lactate Dehydrogenase (Cytochrome)Membrane PotentialsMitochondriaProtein ConformationProtein PrecursorsProtein Processing, Post-TranslationalRecombinant Fusion ProteinsSaccharomyces cerevisiaeTetrahydrofolate DehydrogenaseConceptsMitochondrial protein uptakeTranslocation contact sitesAmino-terminal thirdStable tertiary structureDihydrofolate reductase domainImport pathwayPreprotein translocationHybrid proteinProtein foldingMitochondrial membraneTranslocation sitesContact sitesCytochrome b2Fusion proteinPolypeptide segmentsYeast cellsReductase domainTertiary structureProtein uptakeDihydrofolate reductaseProteinMitochondriaMembraneVivoFolding
1989
Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
Ostermann J, Horwich A, Neupert W, Hartl F. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 1989, 341: 125-130. PMID: 2528694, DOI: 10.1038/341125a0.Peer-Reviewed Original Research