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 removalAntifolding 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
A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
Trent J, Nimmesgern E, Wall J, Hartl F, Horwich A. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 1991, 354: 490-493. PMID: 1836250, DOI: 10.1038/354490a0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceAnimalsArchaeal ProteinsBacterial ProteinsBase SequenceDNA-Binding ProteinsHeat-Shock ProteinsIntracellular Signaling Peptides and ProteinsMiceMicrotubule-Associated ProteinsMolecular ChaperonesMolecular Sequence DataNuclear ProteinsSaccharomyces cerevisiaeSequence Homology, Nucleic AcidSulfolobusT-Complex Genome RegionTemperatureUbiquitin-Protein LigasesConceptsComplex polypeptide 1Molecular chaperonesEukaryotic cytosolThermophilic archaebacteriumPolypeptide 1Ubiquitous eukaryotic proteinThermophilic factor 55Homo-oligomeric complexesMajor heat shock proteinsHeat shock proteinsChaperone componentsEukaryotic proteinsEssential proteinsProtein TAbundant proteinsSulfolobus shibataeComplex bindsS. shibataeChaperonesPrimary structureTF55ChaperoninProteinArchaebacteriaTCP1
1990
Sorting pathways of mitochondrial inner membrane proteins
MAHLKE K, PFANNER N, MARTIN J, HORWICH A, HARTL F, NEUPERT W. Sorting pathways of mitochondrial inner membrane proteins. The FEBS Journal 1990, 192: 551-555. PMID: 2145157, DOI: 10.1111/j.1432-1033.1990.tb19260.x.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBiological EvolutionDNA, FungalHeat-Shock ProteinsIntracellular MembranesMitochondrial ADP, ATP TranslocasesMolecular Sequence DataNeurospora crassaOligonucleotide ProbesProtein Processing, Post-TranslationalProton-Translocating ATPasesRecombinant Fusion ProteinsSubmitochondrial ParticlesConceptsMitochondrial inner membrane proteinADP/ATP carrierInner membrane proteinMembrane proteinsATP carrierTargeting signalsNuclear-encoded mitochondrial inner membrane proteinsAmino-terminal targeting signalsNuclear-encoded mitochondrial proteinsDifferent import receptorsMitochondrial precursor proteinsHeat shock protein Hsp60Precursor proteinProkaryotic equivalentProkaryotic ancestorsEndosymbiont hypothesisImport receptorSubunit 9Sorting pathwaysMitochondrial proteinsInner membraneF0-ATPaseMitochondrial matrixAssembly pathwayMitochondrial membrane
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
1985
A 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 cellsLocalization of DNA sequences in region Xp21 of the human X chromosome: search for molecular markers close to the Duchenne muscular dystrophy locus.
de Martinville B, Kunkel L, Bruns G, Morlé F, Koenig M, Mandel J, Horwich A, Latt S, Gusella J, Housman D. Localization of DNA sequences in region Xp21 of the human X chromosome: search for molecular markers close to the Duchenne muscular dystrophy locus. American Journal Of Human Genetics 1985, 37: 235-49. PMID: 2984924, PMCID: PMC1684559.Peer-Reviewed Original ResearchConceptsX chromosomeHuman X chromosome short armSomatic cell hybrid linesMolecular markersShort armX chromosome short armHuman X chromosomeChromosome short armDNA sequence mapGene dosage studiesOrnithine transcarbamylase geneAbnormal X chromosomeDNA sequencesDNA fragmentsHybrid linesChromosomesSequence mapsMuscular dystrophyStructural rearrangementsHuman lymphoblastsBand Xp21Duchenne muscular dystrophyGenesLociXp21
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
1983
Molecular cloning of the cDNA coding for rat ornithine transcarbamoylase.
Horwich A, Kraus J, Williams K, Kalousek F, Konigsberg W, Rosenberg L. Molecular cloning of the cDNA coding for rat ornithine transcarbamoylase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1983, 80: 4258-4262. PMID: 6576335, PMCID: PMC384016, DOI: 10.1073/pnas.80.14.4258.Peer-Reviewed Original ResearchConceptsOrnithine transcarbamoylaseSequential Edman analysesCDNA probeMitochondrial matrix enzymeInsertion of cDNAAmino acid residuesConsecutive amino acid residuesCarboxyl-terminal portionCytoplasmic polysomesMolecular cloningCDNA clonesEdman analysisDifferential colony hybridizationTranslation assaysX chromosomeCDNA codingMatrix enzymeEnzyme subunitMessenger speciesAcid residuesSequence presentPolysome immunoadsorptionIdentical subunitsColony hybridizationEscherichia coli