2000
Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL
Farr G, Furtak K, Rowland M, Ranson N, Saibil H, Kirchhausen T, Horwich A. Multivalent Binding of Nonnative Substrate Proteins by the Chaperonin GroEL. Cell 2000, 100: 561-573. PMID: 10721993, DOI: 10.1016/s0092-8674(00)80692-3.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBacterial ProteinsBinding SitesCattleChaperonin 10Chaperonin 60Chemical PhenomenaChemistry, PhysicalCryoelectron MicroscopyCystineEscherichia coliEthylmaleimideImage Processing, Computer-AssistedMacromolecular SubstancesMalate DehydrogenaseModels, MolecularPeptidesProtein BindingProtein ConformationProtein FoldingProtein Structure, TertiaryRibulose-Bisphosphate CarboxylaseStructure-Activity RelationshipThiosulfate SulfurtransferaseConceptsNonnative substrate proteinApical domainSubstrate proteinsChaperonin GroELWild-type domainCross-linking experimentsCochaperonin GroESNonnative proteinsProductive foldingGroEL ringSingle polypeptideHydrophobic residuesMalate dehydrogenaseBinary complex formationRubiscoProteinInside aspectMultivalent bindingGroELCentral cavityComplex formationBindingDomainGroESOpen ring
1998
[11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL
Horwich A, Burston S, Rye H, Weissman J, Fenton W. [11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL. Methods In Enzymology 1998, 290: 141-146. PMID: 9534157, DOI: 10.1016/s0076-6879(98)90013-1.Peer-Reviewed Original ResearchConceptsBacterial chaperonin GroELGreen fluorescent proteinChaperonin GroELDouble-ring assemblyAddition of GroESDouble-ring complexesSingle-ring versionUnliganded GroELBacterial chaperoninsGroEL ringNeighboring subunitProtein foldsGroELEquatorial domainNonnative formsFluorescent proteinGroESNative stateNative formCentral channelCritical signalingSubunitsSignalingForm contactsNormal ATP
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
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 denaturationOrganellesDenaturationRefolding
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