2001
GroEL/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 Research
1993
Protein 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 ResearchProtein 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. 1993, 57-70. DOI: 10.1007/978-94-011-2108-8_8.Peer-Reviewed Original Research
1992
Antifolding 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 reductaseProteinMitochondriaMembraneVivoFolding
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
Import 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
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 cleavageTranscarbamoylaseResiduesMitochondria