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 removal
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