2023
Species-specific protein–protein interactions govern the humanization of the 20S proteasome in yeast
Sultana S, Abdullah M, Li J, Hochstrasser M, Kachroo A. Species-specific protein–protein interactions govern the humanization of the 20S proteasome in yeast. Genetics 2023, 225: iyad117. PMID: 37364278, PMCID: PMC10471208, DOI: 10.1093/genetics/iyad117.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsYeast proteasomeLocal protein-protein interactionsSpecific protein-protein interactionsYeast proteasome subunitsVast evolutionary distancesC-terminal tailFull-length tailThousands of genesHigh-throughput pipelineYeast counterpartEvolutionary divergenceEvolutionary distanceAssembly intermediatesHuman genesProteasome subunitsComplementationProteasomeSubunitsYeastGenesDistinct interactionsCore assemblyHuman β3Β3 subunitMolecular Biology of Cytoplasmic Incompatibility Caused by Wolbachia Endosymbionts
Hochstrasser M. Molecular Biology of Cytoplasmic Incompatibility Caused by Wolbachia Endosymbionts. Annual Review Of Microbiology 2023, 77: 299-316. PMID: 37285552, DOI: 10.1146/annurev-micro-041020-024616.Peer-Reviewed Original ResearchConceptsCytoplasmic incompatibilityMale killingHost ubiquitin systemEndosymbiotic bacteriaFemale germlineEukaryotic cellsCognate partnersEmbryonic lethalityBicistronic operonUbiquitin systemDownstream genesWolbachia endosymbiontReproductive advantageCI inductionMolecular biologyInfected femalesEndosymbiontsInfections of malesReproductive alterationsDeubiquitylaseDeubiquitylasesOperonParthenogenesisArthropodsGermline
2022
Orientia tsutsugamushi OtDUB Is Expressed and Interacts with Adaptor Protein Complexes during Infection
Adcox H, Berk J, Hochstrasser M, Carlyon J. Orientia tsutsugamushi OtDUB Is Expressed and Interacts with Adaptor Protein Complexes during Infection. Infection And Immunity 2022, 90: e00469-22. PMID: 36374099, PMCID: PMC9753657, DOI: 10.1128/iai.00469-22.Peer-Reviewed Original ResearchConceptsObligate intracellular lifestyleClathrin adaptor protein complex 1Adaptor protein complex 1Non-integral membrane proteinsAdaptor protein complexesHost endocytic pathwayMembrane traffic regulatorsCell wall proteinsWall proteinsProtein complexesIntracellular lifestyleRho GTPasesAdapter proteinEndocytic pathwayMembrane proteinsUbiquitin bindingCellular pathwaysCell wallStructured illumination microscopyPhospholipid phosphatidylserineIntact bacteriaO. tsutsugamushi infectionProteinRecombinant versionInteractome
2001
SP-RING for SUMO New Functions Bloom for a Ubiquitin-like Protein
Hochstrasser M. SP-RING for SUMO New Functions Bloom for a Ubiquitin-like Protein. Cell 2001, 107: 5-8. PMID: 11595179, DOI: 10.1016/s0092-8674(01)00519-0.Peer-Reviewed Original Research
2000
The Doa4 Deubiquitinating Enzyme Is Functionally Linked to the Vacuolar Protein-sorting and Endocytic Pathways
Amerik A, Nowak J, Swaminathan S, Hochstrasser M. The Doa4 Deubiquitinating Enzyme Is Functionally Linked to the Vacuolar Protein-sorting and Endocytic Pathways. Molecular Biology Of The Cell 2000, 11: 3365-3380. PMID: 11029042, PMCID: PMC14998, DOI: 10.1091/mbc.11.10.3365.Peer-Reviewed Original ResearchMeSH KeywordsAdenocarcinomaAmino Acid SequenceBreast NeoplasmsCysteine EndopeptidasesEndocytosisEndopeptidasesEndosomal Sorting Complexes Required for TransportFemaleFungal ProteinsGenotypeHumansMolecular Sequence DataMultienzyme ComplexesMutagenesisProteasome Endopeptidase ComplexRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Homology, Amino AcidSubstrate SpecificitySuppression, GeneticUbiquitin ThiolesteraseUbiquitinsVacuolesConceptsPrevacuolar compartmentDeubiquitinating enzymeVacuolar protein sorting (VPS) pathwayFluorescent proteinEndomembrane protein traffickingProtein sorting pathwaysUbiquitinated membrane proteinsVacuolar protein sortingClass E compartmentSpontaneous extragenic suppressorsGreen fluorescent proteinExtragenic suppressorsProtein sortingProtein traffickingProtein deubiquitinationUbiquitin recyclingPathway substrateE compartmentMembrane proteinsEndocytic pathwayUbiquitinated intermediatesDifferent genesMultivesicular bodiesNuclear distributionUnanticipated connectionsEvolution and function of ubiquitin-like protein-conjugation systems
Hochstrasser M. Evolution and function of ubiquitin-like protein-conjugation systems. Nature Cell Biology 2000, 2: e153-e157. PMID: 10934491, DOI: 10.1038/35019643.Peer-Reviewed Original Research
1999
Substrate Targeting in the Ubiquitin System
Laney J, Hochstrasser M. Substrate Targeting in the Ubiquitin System. Cell 1999, 97: 427-430. PMID: 10338206, DOI: 10.1016/s0092-8674(00)80752-7.Peer-Reviewed Original ResearchA 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
1998
Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle
Finley D, Tanaka K, Mann C, Feldmann H, Hochstrasser M, Vierstra R, Johnston S, Hampton R, Haber J, McCusker J, Silver P, Frontali L, Thorsness P, Varshavsky A, Byers B, Madura K, Reed S, Wolf D, Jentsch S, Sommer T, Baumeister W, Goldberg A, Fried V, Rubin D, Glickman M, Toh-e A. Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle. Trends In Biochemical Sciences 1998, 23: 244-245. PMID: 9697412, DOI: 10.1016/s0968-0004(98)01222-5.Peer-Reviewed Original ResearchAn Evolutionarily Conserved Gene on Human Chromosome 5q33–q34,UBH1,Encodes a Novel Deubiquitinating Enzyme
Hansen-Hagge T, Janssen J, Hameister H, Papa F, Zechner U, Seriu T, Jauch A, Becke D, Hochstrasser M, Bartram C. An Evolutionarily Conserved Gene on Human Chromosome 5q33–q34,UBH1,Encodes a Novel Deubiquitinating Enzyme. Genomics 1998, 49: 411-418. PMID: 9615226, DOI: 10.1006/geno.1998.5275.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansChromosome MappingChromosomes, Human, Pair 14Chromosomes, Human, Pair 5Conserved SequenceDNA PrimersEndopeptidasesEvolution, MolecularHumansIn Situ HybridizationLeukemiaMiceMolecular Sequence DataMultigene FamilyNervous SystemNeuronsPolymerase Chain ReactionPseudogenesSaccharomyces cerevisiaeSequence AlignmentSequence Homology, Amino AcidTranscription, GeneticTranslocation, GeneticUbiquitin ThiolesteraseConceptsGene familyDeubiquitinating enzymeNovel multigene familyGalactosidase fusion proteinSitu hybridizationNovel deubiquitinating enzymeNorthern blot analysisConserved geneCaenorhabditis elegansHypothetical proteinsMultigene familyHuman genesLow-level expressionFunctional membersHuman chromosomesProtein displayFusion proteinMouse tissuesEscherichia coliChromosome 5q33Blot analysisBreakpoint sequencesEnzyme 1GenesEnzyme
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
1995
Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
Hochstrasser M. Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Current Opinion In Cell Biology 1995, 7: 215-223. PMID: 7612274, DOI: 10.1016/0955-0674(95)80031-x.Peer-Reviewed Original ResearchConceptsCellular regulatory mechanismsIntracellular protein degradationCell cycle progressionProtein ubiquitinationUbiquitin systemProtein degradationRegulatory mechanismsCycle progressionSpecific proteinsForeign proteinsLarge familyCell proliferationProteasomeRapid degradationProteinClass I MHC moleculesUbiquitinationDeubiquitinationUbiquitinI MHC moleculesProteolysisEnzymeKey stepDegradationRegulation
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 ThiolesteraseUbiquitins
1992
Ubiquitin and intracellular protein degradation
Hochstrasser M. Ubiquitin and intracellular protein degradation. Current Opinion In Cell Biology 1992, 4: 1024-1031. PMID: 1336669, DOI: 10.1016/0955-0674(92)90135-y.Peer-Reviewed Original ResearchConceptsEukaryotic cell regulationConjugation of ubiquitinUbiquitin systemProteolytic targetingProtein degradationIntracellular proteinsProtein turnoverCell regulationDiverse arrayUbiquitinCentral roleProteinEukaryotesMajor routeUbiquitinationProteaseEnzymeDegradationPathwayRegulationRecent workTargetingTurnoverPeptides