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 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 proteins
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