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
1999
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
Weber-Ban E, Reid B, Miranker A, Horwich A. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature 1999, 401: 90-93. PMID: 10485712, DOI: 10.1038/43481.Peer-Reviewed Original ResearchConceptsSubstrate proteinsATP-dependent degradationGreen fluorescent protein GFPHydrogen exchange experimentsStable monomeric proteinFluorescent protein GFPNon-native formsChaperone ClpAChaperone familyEukaryotic proteinsProtease ClpPPresence of ATPChaperonin GroELHexameric ringClpAProteasome functionProtein GFPProtein structureMonomeric proteinNative proteinGlobal unfoldingProteinCentral channelRecognition peptideClpAP
1994
Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell
Craig E, Weissman J, Horwich A. Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell. Cell 1994, 78: 365-372. PMID: 7914834, DOI: 10.1016/0092-8674(94)90416-2.Peer-Reviewed Original ResearchGroEL-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
1993
Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
Horwich A, Low K, Fenton W, Hirshfield I, Furtak K. Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL. Cell 1993, 74: 909-917. PMID: 8104102, DOI: 10.1016/0092-8674(93)90470-b.Peer-Reviewed Original ResearchMeSH KeywordsATP-Binding Cassette TransportersBacterial ProteinsBacteriophage lambdaCarrier ProteinsChaperonin 60Citrate (si)-SynthaseEscherichia coliEscherichia coli ProteinsHeat-Shock ProteinsKetoglutarate Dehydrogenase ComplexMaltoseMaltose-Binding ProteinsMethionineMonosaccharide Transport ProteinsOperonOrnithine CarbamoyltransferasePlasmidsPolyribonucleotide NucleotidyltransferasePromoter Regions, GeneticProtein BiosynthesisProtein FoldingProtein Sorting SignalsSequence DeletionTemperatureTransduction, GeneticConceptsCytoplasmic proteinsTemperature-sensitive lethal mutationBacterial cytoplasmic proteinsE. coli chaperonin GroELMaltose-binding proteinRole of GroELNative tertiary structureEssential genesChaperonin GroELBacterial cytoplasmMutant cellsLethal mutationsNonpermissive temperatureGenetic informationPolynucleotide phosphorylaseGeneral translationTertiary structureCitrate synthasePathways of transferKetoglutarate dehydrogenaseGeneral roleGroELNative conformationProteinTest proteinsA polypeptide bound by the chaperonin groEL is localized within a central cavity.
Braig K, Simon M, Furuya F, Hainfeld J, Horwich A. A polypeptide bound by the chaperonin groEL is localized within a central cavity. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 3978-3982. PMID: 8097882, PMCID: PMC46429, DOI: 10.1073/pnas.90.9.3978.Peer-Reviewed Original ResearchConceptsChaperonin GroELGroEL complexEscherichia coli chaperonin GroELOligomeric protein complexesDihydrofolate reductaseMolten globule-like intermediateCentral cavityPolypeptide chain foldingChaperonin ringsChaperonin complexProtein complexesCellular compartmentsDHFR moleculeMonomeric membersPresence of MgATPGroELNative stateEssential roleCompact conformationPolypeptideComplexesCochaperoninChaperoninMultiple sitesIntermediatesProtein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1
Horwich A, Willison K. Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1. Philosophical Transactions Of The Royal Society B Biological Sciences 1993, 339: 313-326. PMID: 8098536, DOI: 10.1098/rstb.1993.0030.Peer-Reviewed Original Research
1992
Prevention of Protein Denaturation Under Heat Stress by the Chaperonin Hsp60
Martin J, Horwich A, Hartl F. Prevention of Protein Denaturation Under Heat Stress by the Chaperonin Hsp60. Science 1992, 258: 995-998. PMID: 1359644, DOI: 10.1126/science.1359644.Peer-Reviewed Original ResearchConceptsDihydrofolate reductaseShock proteinsMitochondrial heat shock protein 60Native dihydrofolate reductaseHeat shock proteinsVariety of polypeptidesPreexisting proteinsChaperonin Hsp60Hsp60 familyEnvironmental stressHeat shock protein 60Shock protein 60Stress conditionsHeat stressProteinGeneral mechanismPhysiological responsesProtein 60HSP60Cellular structureThermal denaturationProtein denaturationOrganellesDenaturationRefoldingAntifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space
Koll H, Guiard B, Rassow J, Ostermann J, Horwich A, Neupert W, Hartl F. Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 1992, 68: 1163-1175. PMID: 1347713, DOI: 10.1016/0092-8674(92)90086-r.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBiological TransportChaperonin 60ChaperoninsFungal ProteinsHeat-Shock ProteinsL-Lactate DehydrogenaseL-Lactate Dehydrogenase (Cytochrome)MitochondriaMolecular Sequence DataProtein ConformationProtein Sorting SignalsProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae
1991
A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
Trent J, Nimmesgern E, Wall J, Hartl F, Horwich A. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 1991, 354: 490-493. PMID: 1836250, DOI: 10.1038/354490a0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceAnimalsArchaeal ProteinsBacterial ProteinsBase SequenceDNA-Binding ProteinsHeat-Shock ProteinsIntracellular Signaling Peptides and ProteinsMiceMicrotubule-Associated ProteinsMolecular ChaperonesMolecular Sequence DataNuclear ProteinsSaccharomyces cerevisiaeSequence Homology, Nucleic AcidSulfolobusT-Complex Genome RegionTemperatureUbiquitin-Protein LigasesConceptsComplex polypeptide 1Molecular chaperonesEukaryotic cytosolThermophilic archaebacteriumPolypeptide 1Ubiquitous eukaryotic proteinThermophilic factor 55Homo-oligomeric complexesMajor heat shock proteinsHeat shock proteinsChaperone componentsEukaryotic proteinsEssential proteinsProtein TAbundant proteinsSulfolobus shibataeComplex bindsS. shibataeChaperonesPrimary structureTF55ChaperoninProteinArchaebacteriaTCP1Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
Martin J, Langer T, Boteva R, Schramel A, Horwich A, Hartl F. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 1991, 352: 36-42. PMID: 1676490, DOI: 10.1038/352036a0.Peer-Reviewed Original ResearchConceptsChaperonin-mediated proteinMolten globule-like intermediateMolten globule stateGroEL proteinProtein monomersMonomeric enzymeProtein structureTertiary structureATP moleculesGlobule stateGeneral mechanismMg-ATPGroESGroELFoldingProteinActive processPolypeptideEnzymeChain foldingConformationVivo
1990
Sorting pathways of mitochondrial inner membrane proteins
MAHLKE K, PFANNER N, MARTIN J, HORWICH A, HARTL F, NEUPERT W. Sorting pathways of mitochondrial inner membrane proteins. The FEBS Journal 1990, 192: 551-555. PMID: 2145157, DOI: 10.1111/j.1432-1033.1990.tb19260.x.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBiological EvolutionDNA, FungalHeat-Shock ProteinsIntracellular MembranesMitochondrial ADP, ATP TranslocasesMolecular Sequence DataNeurospora crassaOligonucleotide ProbesProtein Processing, Post-TranslationalProton-Translocating ATPasesRecombinant Fusion ProteinsSubmitochondrial ParticlesConceptsMitochondrial inner membrane proteinADP/ATP carrierInner membrane proteinMembrane proteinsATP carrierTargeting signalsNuclear-encoded mitochondrial inner membrane proteinsAmino-terminal targeting signalsNuclear-encoded mitochondrial proteinsDifferent import receptorsMitochondrial precursor proteinsHeat shock protein Hsp60Precursor proteinProkaryotic equivalentProkaryotic ancestorsEndosymbiont hypothesisImport receptorSubunit 9Sorting pathwaysMitochondrial proteinsInner membraneF0-ATPaseMitochondrial matrixAssembly pathwayMitochondrial membraneProtein import into mitochondria and peroxisomes
Horwich A. Protein import into mitochondria and peroxisomes. Current Opinion In Cell Biology 1990, 2: 625-633. PMID: 1979227, DOI: 10.1016/0955-0674(90)90103-l.Peer-Reviewed Original ResearchProtein-catalysed protein folding
Horwich A, Neupert W, Hartl F. Protein-catalysed protein folding. Trends In Biotechnology 1990, 8: 126-131. PMID: 1369433, DOI: 10.1016/0167-7799(90)90153-o.Peer-Reviewed Original Research
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 ResearchMitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
Cheng M, Hartl F, Martin J, Pollock R, Kalousek F, Neuper W, Hallberg E, Hallberg R, Horwich A. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 1989, 337: 620-625. PMID: 2645524, DOI: 10.1038/337620a0.Peer-Reviewed Original ResearchMeSH KeywordsFungal ProteinsGenesGenes, FungalHeat-Shock ProteinsMitochondriaMutationPlasmidsProtein Processing, Post-TranslationalSaccharomyces cerevisiae