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
1992
Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein.
West A, Clark D, Martin J, Neupert W, Hartl F, Horwich A. Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein. Journal Of Biological Chemistry 1992, 267: 24625-24633. PMID: 1447206, DOI: 10.1016/s0021-9258(18)35810-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceChromosomes, FungalDNA, FungalGenes, FungalGenes, LethalGenes, SuppressorGenotypeMitochondriaMolecular Sequence DataMutationOpen Reading FramesPeptidesPlasmidsProtein ConformationRestriction MappingSaccharomyces cerevisiaeSequence DeletionSequence Homology, Amino AcidSuppression, GeneticTemperatureConceptsProtein importHydrophobic proteinsNH2-terminal signal peptideYeast genomic libraryNonfermentable carbon sourcesProteins of mitochondriaMitochondrial membrane proteinPrecursor proteinHigh-copy plasmidMitochondrial processingProtein translocationGenomic libraryPEP geneGrowth defectChromosomal genesMembrane proteinsMitochondrial matrixSignal peptideGenetic suppressionLethal mutationsMitochondrial membraneDouble disruptionRelated genesSequence analysisProteolytic removalPrevention 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
Protein folding causes an arrest of preprotein translocation into mitochondria in vivo.
Wienhues U, Becker K, Schleyer M, Guiard B, Tropschug M, Horwich A, Pfanner N, Neupert W. Protein folding causes an arrest of preprotein translocation into mitochondria in vivo. Journal Of Cell Biology 1991, 115: 1601-1609. PMID: 1757464, PMCID: PMC2289212, DOI: 10.1083/jcb.115.6.1601.Peer-Reviewed Original ResearchMeSH KeywordsAminopterinBiological TransportIntracellular MembranesKineticsL-Lactate DehydrogenaseL-Lactate Dehydrogenase (Cytochrome)Membrane PotentialsMitochondriaProtein ConformationProtein PrecursorsProtein Processing, Post-TranslationalRecombinant Fusion ProteinsSaccharomyces cerevisiaeTetrahydrofolate DehydrogenaseConceptsMitochondrial protein uptakeTranslocation contact sitesAmino-terminal thirdStable tertiary structureDihydrofolate reductase domainImport pathwayPreprotein translocationHybrid proteinProtein foldingMitochondrial membraneTranslocation sitesContact sitesCytochrome b2Fusion proteinPolypeptide segmentsYeast cellsReductase domainTertiary structureProtein uptakeDihydrofolate reductaseProteinMitochondriaMembraneVivoFoldingMitochondrial protein import.
Horwich A, Cheng M, West A, Pollock R. Mitochondrial protein import. Current Topics In Microbiology And Immunology 1991, 170: 1-42. PMID: 1760928, DOI: 10.1007/978-3-642-76389-2_1.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological Transport, ActiveHumansMitochondriaProtein Sorting SignalsProteinsSubmitochondrial ParticlesConceptsMitochondrial protein import pathwayProtein import pathwayPrecise molecular functionConformational alterationsImport pathwayMolecular functionsStep of recognitionMembrane translocationProteolytic cleavageProteinTranslocationDynamic picturePowerful toolGeneticsAlterationsPathwayBiochemistryCleavageCritical features
1990
Protein 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 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 Research
1988
The processing peptidase of yeast mitochondria: the two co‐operating components MPP and PEP are structurally related.
Pollock R, Hartl F, Cheng M, Ostermann J, Horwich A, Neupert W. The processing peptidase of yeast mitochondria: the two co‐operating components MPP and PEP are structurally related. The EMBO Journal 1988, 7: 3493-3500. PMID: 3061797, PMCID: PMC454850, DOI: 10.1002/j.1460-2075.1988.tb03225.x.Peer-Reviewed Original ResearchConceptsMitochondrial processing peptidaseMitochondrial precursor proteinsProcessing peptidasePrecursor proteinMutant of SaccharomycesRemarkable sequence similarityYeast mitochondriaMPP geneSequence similarityHydrophilic proteinNovel peptidaseAmino acidsProteolytic cleavageProteinPeptidaseMutantsMitochondriaCommon originPresequenceSaccharomycesPEPGenesMutationsCleavageFunction
1987
The ornithine transcarbamylase leader peptide directs mitochondrial import through both its midportion structure and net positive charge.
Horwich A, Kalousek F, Fenton W, Furtak K, Pollock R, Rosenberg L. The ornithine transcarbamylase leader peptide directs mitochondrial import through both its midportion structure and net positive charge. Journal Of Cell Biology 1987, 105: 669-677. PMID: 3624306, PMCID: PMC2114782, DOI: 10.1083/jcb.105.2.669.Peer-Reviewed Original ResearchImport and processing of human ornithine transcarbamoylase precursor by mitochondria from Saccharomyces cerevisiae.
Cheng M, Pollock R, Hendrick J, Horwich A. Import and processing of human ornithine transcarbamoylase precursor by mitochondria from Saccharomyces cerevisiae. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 4063-4067. PMID: 3295876, PMCID: PMC305022, DOI: 10.1073/pnas.84.12.4063.Peer-Reviewed Original ResearchConceptsMitochondrial membraneEnzymatic activityNH2-terminal leader peptideMitochondrial matrix fractionWild-type precursorS. cerevisiae strainMitochondrial importMammalian mitochondriaMature subunitSubunit precursorOperon promoterS. cerevisiaeSelective growth conditionsLeader peptideYeast cellsArtificial mutationsOTCase activityMatrix fractionOrnithine transcarbamoylaseCerevisiae strainSaccharomycesGrowth conditionsMatrix compartmentMitochondriaSubunits
1986
Targeting of Nuclear‐Encoded Proteins to the Mitochondrial Matrix: Implications for Human Genetic Defects
ROSENBERG L, FENTON W, HORWICH A, KALOUSEK F, KRAUS J. Targeting of Nuclear‐Encoded Proteins to the Mitochondrial Matrix: Implications for Human Genetic Defects. Annals Of The New York Academy Of Sciences 1986, 488: 99-108. PMID: 3472484, DOI: 10.1111/j.1749-6632.1986.tb54396.x.Peer-Reviewed Original ResearchTargeting of pre-ornithine transcarbamylase to mitochondria: Definition of critical regions and residues in the leader peptide
Horwich A, Kalousek F, Fenton W, Pollock R, Rosenberg L. Targeting of pre-ornithine transcarbamylase to mitochondria: Definition of critical regions and residues in the leader peptide. Cell 1986, 44: 451-459. PMID: 3943133, DOI: 10.1016/0092-8674(86)90466-6.Peer-Reviewed Original Research
1985
Arginine in the leader peptide is required for both import and proteolytic cleavage of a mitochondrial precursor.
Horwich A, Kalousek F, Rosenberg L. Arginine in the leader peptide is required for both import and proteolytic cleavage of a mitochondrial precursor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 4930-4933. PMID: 3895227, PMCID: PMC390471, DOI: 10.1073/pnas.82.15.4930.Peer-Reviewed Original ResearchConceptsLeader peptideOrnithine transcarbamoylaseImport of precursorsMost mitochondrial proteinsMitochondrial matrix fractionOverall amino acid compositionMitochondrial matrix enzymeMitochondrial precursorsMitochondrial proteinsSubunit precursorAmino acid compositionBasic arginine residuesBasic residuesMatrix enzymeGlycine residueLarger precursorArginine residuesMatrix fractionIntact mitochondriaNH2-terminalDependent proteaseProteolytic cleavageTranscarbamoylaseResiduesMitochondriaExpression of amplified DNA sequences for ornithine transcarbamylase in HeLa cells: arginine residues may be required for mitochondrial import of enzyme precursor.
Horwich A, Fenton W, Firgaira F, Fox J, Kolansky D, Mellman I, Rosenberg L. Expression of amplified DNA sequences for ornithine transcarbamylase in HeLa cells: arginine residues may be required for mitochondrial import of enzyme precursor. Journal Of Cell Biology 1985, 100: 1515-1521. PMID: 3988798, PMCID: PMC2113848, DOI: 10.1083/jcb.100.5.1515.Peer-Reviewed Original ResearchConceptsMitochondrial importOTC precursorsHeLa cellsOrnithine transcarbamylaseArginine residuesMouse dihydrofolate reductaseNH2-terminal leader sequenceRate of importArginine analog canavanineViral regulatory elementsImmunoprecipitation of extractsMitochondrial localizationCDNA sequenceRegulatory elementsLeader sequenceDNA sequencesEnzyme precursorsMitochondrial enzymesCell extractsDihydrofolate reductaseEnzymatic activityBlot analysisNormal precursorsResiduesSubunitsA leader peptide is sufficient to direct mitochondrial import of a chimeric protein.
Horwich A, Kalousek F, Mellman I, Rosenberg L. A leader peptide is sufficient to direct mitochondrial import of a chimeric protein. The EMBO Journal 1985, 4: 1129-1135. PMID: 3891325, PMCID: PMC554314, DOI: 10.1002/j.1460-2075.1985.tb03750.x.Peer-Reviewed Original ResearchConceptsChimeric precursor proteinsMitochondrial importLeader peptideChimeric precursorsDihydrofolate reductaseMost mitochondrial proteinsPost-translational importMutant CHO cell linesCloned nucleotide sequencePrecursor proteinOrnithine transcarbamylaseCell-free systemCHO cell linesEnzyme dihydrofolate reductaseMitochondrial proteinsMitochondrial localizationRegulatory elementsLeader sequenceNucleotide sequenceStable transformantsAdditional proteinsSelectable markerChimeric proteinLarger precursorIntact cells
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