2023
Proteasomes: Isolation and Activity Assays
Li Y, Tomko R, Hochstrasser M. Proteasomes: Isolation and Activity Assays. Current Protocols 2023, 3: e717. PMID: 37026813, PMCID: PMC10337785, DOI: 10.1002/cpz1.717.Peer-Reviewed Original ResearchConceptsRegulatory particleOne-step purification schemeCore particlesMultisubunit protease complexUbiquitin-proteasome systemUbiquitin polypeptidesUnneeded proteinsYeast SaccharomycesProtein substratesProtease complexProteasomeGel filtration stepPurification schemeProteolytic activityEukaryotesSaccharomycesPolypeptideProteinSubstrateAssaysComplexes
2000
A viable ubiquitin‐activating enzyme mutant for evaluating ubiquitin system function in Saccharomyces cerevisiae
Swanson R, Hochstrasser M. A viable ubiquitin‐activating enzyme mutant for evaluating ubiquitin system function in Saccharomyces cerevisiae. FEBS Letters 2000, 477: 193-198. PMID: 10908719, DOI: 10.1016/s0014-5793(00)01802-0.Peer-Reviewed Original ResearchConceptsUbiquitin system functionActivation of ubiquitinUbiquitin-activating enzymeProteasome-independent degradationUbiquitin systemCellular processesPathway substrateMammalian cellsHypomorphic alleleProtein modificationEnzyme mutantsMutant allelesMembrane receptorsMutantsUbiquitinComparable mutantsSaccharomycesCell functionAllelesProteasomeYeastProteinEnzymeDegradationE1
1999
Interaction of the Doa4 Deubiquitinating Enzyme with the Yeast 26S Proteasome
Papa F, Amerik A, Hochstrasser M. Interaction of the Doa4 Deubiquitinating Enzyme with the Yeast 26S Proteasome. Molecular Biology Of The Cell 1999, 10: 741-756. PMID: 10069815, PMCID: PMC25199, DOI: 10.1091/mbc.10.3.741.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCysteine EndopeptidasesEndopeptidasesEndosomal Sorting Complexes Required for TransportFungal ProteinsMolecular Sequence DataMultienzyme ComplexesProteasome Endopeptidase ComplexRecombinant ProteinsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidStructure-Activity RelationshipUbiquitin ThiolesteraseYeastsConceptsRemoval of ubiquitinUbiquitin-proteasome pathwayYeast 26S ProteasomeProteasome bindingGenetic interactionsProteasome mutationsDoa4Protein substratesCatalytic domainDeubiquitinating enzymeUbp5Physical associationProteolytic intermediatesProteasomeN-terminalFunctional interactionEnzymeRecombination methodRapid degradationMutationsPurification procedurePathwaySubstrate breakdownCopurifiesSaccharomyces
1998
Degradation Signal Masking by Heterodimerization of MATα2 and MATa1 Blocks Their Mutual Destruction by the Ubiquitin-Proteasome Pathway
Johnson P, Swanson R, Rakhilina L, Hochstrasser M. Degradation Signal Masking by Heterodimerization of MATα2 and MATa1 Blocks Their Mutual Destruction by the Ubiquitin-Proteasome Pathway. Cell 1998, 94: 217-227. PMID: 9695950, DOI: 10.1016/s0092-8674(00)81421-x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCysteine EndopeptidasesDimerizationDiploidyFungal ProteinsHaploidyIntramolecular TransferasesLipoproteinsMating FactorMolecular Sequence DataMultienzyme ComplexesMutationPeptidesPheromonesProteasome Endopeptidase ComplexProtein Structure, SecondarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinsConceptsUbiquitin-proteasome pathwayDegradation signalCoiled-coil interactionsAlpha haploid cellsRegulated turnoverMultiprotein complexesHaploid cellsPathway substrateTranscription factorsExtensive mutagenesisProteolytic signalMolecular mechanismsCell typesHeterodimerizationSuch regulationCritical determinantPathwayAlpha2MATa1MATα2Signal maskingRepressorHaploidsSaccharomycesMutagenesis