1999
A new protease required for cell-cycle progression in yeast
Li S, Hochstrasser M. A new protease required for cell-cycle progression in yeast. Nature 1999, 398: 246-251. PMID: 10094048, DOI: 10.1038/18457.Peer-Reviewed Original ResearchMeSH KeywordsCarrier ProteinsCell Cycle ProteinsCloning, MolecularCysteine EndopeptidasesEscherichia coliFungal ProteinsG2 PhaseHumansMitosisMolecular Sequence DataMutagenesisRecombinant Fusion ProteinsRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSmall Ubiquitin-Related Modifier ProteinsSubstrate SpecificitySUMO-1 ProteinUbiquitinsConceptsSUMO-1Cell cycleUbl-specific proteasesUbiquitin-like proteinCell cycle progressionG2/M phaseProtein functionSmt3Cellular proteinsDeubiquitinating enzymeUlp1Distant similarityUbiquitinHuman pathogensM phaseProteinEssential roleNew proteaseProteaseViral proteaseProtein conjugationEukaryotesMutantsUBLYeast
1993
The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
Papa F, Hochstrasser M. The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature 1993, 366: 313-319. PMID: 8247125, DOI: 10.1038/366313a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceEndopeptidasesEndosomal Sorting Complexes Required for TransportFungal ProteinsGenes, FungalHumansMiceMice, NudeMolecular Sequence DataMutationOncogene ProteinsOncogene Proteins, FusionOncogenesOpen Reading FramesPhenotypeProto-Oncogene ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidUbiquitin ThiolesteraseUbiquitinsMultiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor
Chen P, Johnson P, Sommer T, Jentsch S, Hochstrasser M. Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor. Cell 1993, 74: 357-369. PMID: 8393731, DOI: 10.1016/0092-8674(93)90426-q.Peer-Reviewed Original ResearchConceptsUbiquitin-conjugatingAttachment of ubiquitinUbiquitin-conjugating enzymeUBC proteinUbiquitination complexMolecular functionsTranscriptional regulatorsUbiquitination pathwayCellular processesSubstrate specificityDegradation signalPhysiological targetsSubstrate selectionCombinatorial mechanismsUnexpected overlapUBC6Intracellular degradationEnzymeProteinAlpha 2PathwayUbc7Deg1RepressorUbiquitin
1990
In vivo degradation of a transcriptional regulator: The yeast α2 repressor
Hochstrasser M, Varshavsky A. In vivo degradation of a transcriptional regulator: The yeast α2 repressor. Cell 1990, 61: 697-708. PMID: 2111732, DOI: 10.1016/0092-8674(90)90481-s.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBeta-GalactosidaseFungal ProteinsGene Expression Regulation, FungalHalf-LifeMacromolecular SubstancesMolecular Sequence DataMutationProtein EngineeringProtein Processing, Post-TranslationalRecombinant Fusion ProteinsRepressor ProteinsSaccharomyces cerevisiaeTranscription FactorsConceptsYeast S. cerevisiaeTranscriptional regulatorsHeteromeric proteinsAlpha 2S. cerevisiaeDegradation signalRegulatory proteinsOligomeric proteinsSame proteinStructural domainsProteinMultiple functionsSubunitsRepressorDistinct mechanismsVivo concentrationsAdditional defectsCerevisiaeMutantsNovel typeDegradationRegulatorPathwayMetabolic instabilityVivo degradation