2001
ATP-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 ResearchClpA 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 studiesHslUV
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
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 complexATPThe crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
Xu Z, Horwich A, Sigler P. The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex. Nature 1997, 388: 741-750. PMID: 9285585, DOI: 10.1038/41944.Peer-Reviewed Original ResearchConceptsGroEL-GroESApical domainCis ringMulti-subunit protein assembliesCo-chaperonin GroESRings of subunitsPeptide-binding residuesChaperonin complexConsumption of ATPProtein foldingGroEL subunitProtein assembliesTrans ringAllosteric mechanismGroESEquatorial domainBloc movementDouble toroidSecond GroESEscherichia coliOutward tiltAsymmetric intermediatesCentral cavitySubunitsInward tilt
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
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 ring
1994
A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12
Burnett B, Horwich A, Low K. A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K-12. Journal Of Bacteriology 1994, 176: 6980-6985. PMID: 7961461, PMCID: PMC197070, DOI: 10.1128/jb.176.22.6980-6985.1994.Peer-Reviewed Original ResearchThe crystal structure of the bacterial chaperonln GroEL at 2.8 Å
Braig K, Otwinowski Z, Hegde R, Boisvert D, Joachimiak A, Horwich A, Sigler P. The crystal structure of the bacterial chaperonln GroEL at 2.8 Å. Nature 1994, 371: 578-586. PMID: 7935790, DOI: 10.1038/371578a0.Peer-Reviewed Original Research
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
1984
Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase
Horwich A, Fenton W, Williams K, Kalousek F, Kraus J, Doolittle R, Konigsberg W, Rosenberg L. Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase. Science 1984, 224: 1068-1074. PMID: 6372096, DOI: 10.1126/science.6372096.Peer-Reviewed Original ResearchConceptsComplementary DNALeader peptideOrnithine transcarbamylaseAmino-terminal leader peptideMost mitochondrial proteinsComplete primary structureHuman ornithine transcarbamylaseFree cytoplasmic ribosomesMitochondrial matrix enzymeCultured HeLa cellsMitochondrial proteinsCytoplasmic ribosomesRegulatory elementsNucleotide sequenceStable transformantsMatrix enzymeAsparagine residuesAcidic residuesLarger precursorMature formPrimary structureProtein occursHeLa cellsEscherichia coliAmino acids