1997
In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome
Amerik A, Swaminathan S, Krantz B, Wilkinson K, Hochstrasser M. In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome. The EMBO Journal 1997, 16: 4826-4838. PMID: 9305625, PMCID: PMC1170118, DOI: 10.1093/emboj/16.16.4826.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCarbon-Nitrogen LyasesEndopeptidasesFungal ProteinsGene Expression Regulation, FungalGenes, FungalHumansImmunoblottingLyasesMolecular Sequence DataMutagenesis, Site-DirectedPeptide HydrolasesPhenotypeProteasome Endopeptidase ComplexProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSubstrate SpecificityUbiquitinsConceptsUnanchored ubiquitin chainsUbiquitin chainsProtein degradationFree ubiquitin chainsUbiquitin-dependent proteolysisWild-type cellsActive site mutantsFree polyubiquitin chainsEukaryotic proteinsFunctional homologComplementation analysisPolyubiquitin chainsSteady-state levelsDeubiquitinating enzymeUbp14Site mutantsIsopeptidase TCellular proteasesYeast cellsProteasomeInhibition of degradationStriking accumulationProteolysisProteinCells
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