2012
3.10 Chaperones and Protein Folding
Horwich A, Buchner J, Smock R, Gierasch L, Saibil H. 3.10 Chaperones and Protein Folding. 2012, 212-237. DOI: 10.1016/b978-0-12-374920-8.00313-1.Peer-Reviewed Original ResearchSubstrate proteinsMolecular chaperonesSolvent-exposed hydrophobic surfaceSmall heat shock proteinsChaperone-bound proteinsProtein binding domainsNon-native conformationsNon-native statesHeat shock proteinsBinding of ATPSpecialized proteinsProtein foldingChaperonesBinding domainsOligomeric assembliesBiophysical methodsShock proteinsConformational changesPolypeptide chainStress conditionsNative stateProteinCurrent understandingFoldingMultimolecular aggregates
2011
The GroEL/GroES Chaperonin Machine
Horwich A, Saibil H. The GroEL/GroES Chaperonin Machine. 2011, 191-207. DOI: 10.1017/cbo9781139003704.012.Peer-Reviewed Original ResearchChaperonin machinePhage infectionKingdoms of lifeATP-dependent proteinEukaryotic organellesBacterial operonsGroE operonMutant cellsDouble-ring architectureProtein foldingCellular metabolismRing assemblyPhage headOperonIdentical subunitsNative stateBroader roleProteinE. coliGenetic deficiencyBiological actionsParticle assemblyAssemblyEubacteriaGroES
2001
Mechanisms 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
1999
Chaperone rings in protein folding and degradation
Horwich A, Weber-Ban E, Finley D. Chaperone rings in protein folding and degradation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 11033-11040. PMID: 10500119, PMCID: PMC34237, DOI: 10.1073/pnas.96.20.11033.Peer-Reviewed Original ResearchConceptsSubstrate proteinsNon-native formsProcess of foldingCellular proteinsDegradation chamberProtein foldingStep of recognitionProteolytic complexRing assemblyDivergent fatesConformational changesNative stateProteinChaperoninFoldingCentral cavityCooperative interactionsATPPolypeptideFateChaperonesCompartmentalizationVital roleMotifProtease
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 stateCDK2ProteinMaturationBiogenesisFolding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins
Kim S, Schilke B, Craig E, Horwich A. Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 12860-12865. PMID: 9789005, PMCID: PMC23633, DOI: 10.1073/pnas.95.22.12860.Peer-Reviewed Original ResearchConceptsOrnithine transcarbamoylaseYeast cytosolic enzymesCytosolic enzymeNative stateCytosolic Hsp70 proteinsGalpha transducinCytosolic chaperoninEukaryotic cytosolYeast Hsp70Chaperone actionPosttranslational mannerYeast cytosolCytosolic proteinsHSP70 proteinHomotrimeric enzymeProteinSpecific activitySTRUCTURE 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 ResearchConceptsProtein foldingNative stateMechanism of chaperoninsCis ternary complexAsymmetric conformational changesFinal native stateNonnative polypeptidesCochaperonin GroESGroEL ringTrans ringATP hydrolysisGenetic informationChaperonin moleculesConformational changesFolding processFoldingTernary complexPolypeptideGroESATPBiochemical investigationsFinal stepChaperoninGroELComplexesChaperone Action in Folding Newly-Translated Cytosolic Proteins in Bacteria and Eukaryotes
Horwich A. Chaperone Action in Folding Newly-Translated Cytosolic Proteins in Bacteria and Eukaryotes. NATO ASI Series 1998, 41-63. DOI: 10.1007/978-3-642-51463-0_4.Peer-Reviewed Original ResearchNon-native conformationsNative statePrimary amino acid sequenceAmino acid sequenceNon-native statesSubstrate proteinsChaperone functionMolecular chaperonesBiogenesis stepsChaperone actionSpecialized proteinsCofactor bindingProtein foldingAction of nucleotidesPathway stepsMutational alterationsCytosolic proteinsAcid sequenceChaperonesSteric informationFolding processSuch hydrophobic interactionsProteinNative formEssential nature[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
1997
Chaperonin-Mediated Folding in the Eukaryotic Cytosol Proceeds through Rounds of Release of Native and Nonnative Forms
Farr G, Scharl E, Schumacher R, Sondek S, Horwich A. Chaperonin-Mediated Folding in the Eukaryotic Cytosol Proceeds through Rounds of Release of Native and Nonnative Forms. Cell 1997, 89: 927-937. PMID: 9200611, DOI: 10.1016/s0092-8674(00)80278-0.Peer-Reviewed Original ResearchConceptsRounds of releaseSubstrate proteinsNonnative formsNative formChaperonin-mediated foldingEukaryotic cytosolic chaperoninATP-dependent foldingIntact Xenopus oocytesCytosolic chaperoninBacterial chaperoninsEukaryotic cytosolChaperoninNative stateXenopus oocytesEssential roleSingle roundFoldingProteinActinTubulinOverall mechanismGroELTransducinCytosolSmall fraction
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