1999
Structure and functional analyses of the 26S proteasome subunits from plants – Plant 26S proteasome
Fu H, Girod P, Doelling J, van Nocker S, Hochstrasser M, Finley D, Vierstra R. Structure and functional analyses of the 26S proteasome subunits from plants – Plant 26S proteasome. Molecular Biology Reports 1999, 26: 137-146. PMID: 10363660, DOI: 10.1023/a:1006926322501.Peer-Reviewed Original ResearchMeSH KeywordsArabidopsisBryopsidaPeptide HydrolasesProteasome Endopeptidase ComplexStructure-Activity RelationshipConceptsProteasome degrades ubiquitinated proteinsUbiquitin fusion degradation (UFD) pathwayStructure/function analysisAAA-ATPase subunitsC-terminal motifDegradation of proteinsRegulatory particle subunitsCore particlesPlant 26SRpn10 geneArabidopsis genesYeast counterpartMoss PhyscomitrellaArabidopsis thalianaPlant hormonesUbiquitin systemProteasome genesDevelopmental programHomologous recombinationProteolytic complexPlant subunitsReverse geneticsUbiquitinated proteinsUbiquitin conjugatesVivo functionInteraction 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
1997
Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation
Arendt C, Hochstrasser M. Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 7156-7161. PMID: 9207060, PMCID: PMC23776, DOI: 10.1073/pnas.94.14.7156.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCysteine EndopeptidasesMultienzyme ComplexesProteasome Endopeptidase ComplexSaccharomyces cerevisiaeStructure-Activity RelationshipSubstrate SpecificityConceptsActive siteN-terminal threonineBeta subunitDistinct peptidase activitiesMost minor effectsSubunit ringDifferent beta subunitsCorresponding threonineActive site formationUbiquitin-dependent proteolysisDegradation of substratesProteasome active sitesYeast proteasomeArchaeal proteasomeDifferent eukaryotesActive-site nucleophileUbiquitin pathwayHeptameric ringsBasic residuesSubunit interactionsAcidic residuesAlpha subunitSubstrateProteasomePeptide substrates