2001
Protein folding taking shape
Horwich A, Fenton W, Rapoport T. Protein folding taking shape. EMBO Reports 2001, 2: 1068-1073. PMID: 11743017, PMCID: PMC1084171, DOI: 10.1093/embo-reports/kve253.Peer-Reviewed Original ResearchATP-Bound States of GroEL Captured by Cryo-Electron Microscopy
Ranson N, Farr G, Roseman A, Gowen B, Fenton W, Horwich A, Saibil H. ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy. Cell 2001, 107: 869-879. PMID: 11779463, DOI: 10.1016/s0092-8674(01)00617-1.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateChaperonin 60Cryoelectron MicroscopyEscherichia coliModels, MolecularProtein BindingProtein FoldingConceptsCryo-electron microscopySalt-bridge contactsGroEL ringGroEL-GroESChaperonin GroELSalt bridge interactionsCryo-EMMolecular machinesADP complexGroELATPRing complexBridge interactionEffect of ATPCooperativityOpposite ringIntermediate domainGroESGeneral insightsComplexesPolypeptideDomainBridge contactsStructural modelAffinityGroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated
Chaudhuri T, Farr G, Fenton W, Rospert S, Horwich A. GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated. Cell 2001, 107: 235-246. PMID: 11672530, DOI: 10.1016/s0092-8674(01)00523-2.Peer-Reviewed Original ResearchFolding 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 ringPolypeptideUnfoldingMechanisms 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
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
1999
GroEL-GroES Cycling ATP and Nonnative Polypeptide Direct Alternation of Folding-Active Rings
Rye H, Roseman A, Chen S, Furtak K, Fenton W, Saibil H, Horwich A. GroEL-GroES Cycling ATP and Nonnative Polypeptide Direct Alternation of Folding-Active Rings. Cell 1999, 97: 325-338. PMID: 10319813, DOI: 10.1016/s0092-8674(00)80742-4.Peer-Reviewed Original Research
1998
Maturation of Human Cyclin E Requires the Function of Eukaryotic Chaperonin CCT
Won K, Schumacher R, Farr G, Horwich A, Reed S. Maturation of Human Cyclin E Requires the Function of Eukaryotic Chaperonin CCT. Molecular And Cellular Biology 1998, 18: 7584-7589. PMID: 9819444, PMCID: PMC109339, DOI: 10.1128/mcb.18.12.7584.Peer-Reviewed Original ResearchConceptsHuman cyclin EChaperonin CCTCyclin EEukaryotic cytosolic chaperonin CCTCytosolic chaperonin CCTEukaryotic chaperonin CCTLarge oligomeric assembliesYeast-based screenG1/S phase transitionCyclin-dependent kinase CDK2ATP-dependent processS phase transitionCCT complexPresence of ATPProteasomal actionCCT functionHuman proteinsKinase CDK2Oligomeric assembliesHuman cellsNative stateCDK2ProteinMaturationBiogenesisSTRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING
Sigler P, Xu Z, Rye H, Burston S, Fenton W, Horwich A. STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING. Annual Review Of Biochemistry 1998, 67: 581-608. PMID: 9759498, DOI: 10.1146/annurev.biochem.67.1.581.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateChaperonin 10Chaperonin 60Models, MolecularPeptidesProtein BindingProtein ConformationProtein FoldingConceptsProtein foldingNative stateMechanism of chaperoninsCis ternary complexAsymmetric conformational changesFinal native stateNonnative polypeptidesCochaperonin GroESGroEL ringTrans ringATP hydrolysisGenetic informationChaperonin moleculesConformational changesFolding processFoldingTernary complexPolypeptideGroESATPBiochemical investigationsFinal stepChaperoninGroELComplexesThe Hsp70 and Hsp60 Chaperone Machines
Bukau B, Horwich A. The Hsp70 and Hsp60 Chaperone Machines. Cell 1998, 92: 351-366. PMID: 9476895, DOI: 10.1016/s0092-8674(00)80928-9.Peer-Reviewed Original Research
1997
Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
Rye H, Burston S, Fenton W, Beechem J, Xu Z, Sigler P, Horwich A. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 1997, 388: 792-798. PMID: 9285593, DOI: 10.1038/42047.Peer-Reviewed Original ResearchConceptsTrans ringProductive foldingGroES complexChaperonin GroELCis ringCo-chaperone GroESDouble-ring complexesCis ternary complexNon-hydrolysable ATPHydrolysis of ATPGroEL functionGroEL-ATPATP bindingEfficient foldingBinds ATPATP hydrolysisGroESMutant formsMalate dehydrogenaseGroELAMP-PNPDouble-ring structureFoldingTernary complexATPGroEL‐Mediated protein folding
Fenton W, Horwich A. GroEL‐Mediated protein folding. Protein Science 1997, 6: 743-760. PMID: 9098884, PMCID: PMC2144759, DOI: 10.1002/pro.5560060401.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateChaperonin 10Chaperonin 60HydrolysisPeptidesProtein BindingProtein FoldingConceptsGroEL-GroESNonnative polypeptidesSubstrate proteinsATP bindingProtein foldingHomologous proteinsNonnative formsPrimary structureConformational changesGroELTernary complexPolypeptideAssociation 5FoldingProteinBindingChaperonesGroESConformationEnergy landscapeRole of hydrophobicityPathway 3RolePathwayComplex C.
1996
Putting a lid on protein folding: structure and function of the co-chaperonin, GroES
Fenton W, Weissman J, Horwich A. Putting a lid on protein folding: structure and function of the co-chaperonin, GroES. Cell Chemical Biology 1996, 3: 157-161. PMID: 8807841, DOI: 10.1016/s1074-5521(96)90257-4.Peer-Reviewed Original Research
1995
Unliganded GroEL at 2.8 Å: structure and functional implications
Sigler P, Horwich A. Unliganded GroEL at 2.8 Å: structure and functional implications. Philosophical Transactions Of The Royal Society B Biological Sciences 1995, 348: 113-119. PMID: 7770481, DOI: 10.1098/rstb.1995.0052.Peer-Reviewed Original ResearchConceptsATP-binding pocketCentral channelUnfolded polypeptidesApical domainThree-dimensional structureExtensive mutagenesisMutational studiesDyad symmetryC-terminusDistinct domainsGroELATP analogBiochemical studiesStructural scaffoldFunctional implicationsHigh saltSubunitsDomainChaperoninGroESMutagenesisEntire lengthCrystal formsPolypeptideSymmetric ringKinesis of polypeptide during GroEL-mediated folding.
Horwich A, Weissman J, Fenton W. Kinesis of polypeptide during GroEL-mediated folding. Cold Spring Harbor Symposia On Quantitative Biology 1995, 60: 435-40. PMID: 8824417, DOI: 10.1101/sqb.1995.060.01.048.Peer-Reviewed Original Research
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
A 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 sitesIntermediates