2000
The Sec61p Complex Mediates the Integration of a Membrane Protein by Allowing Lipid Partitioning of the Transmembrane Domain
Heinrich S, Mothes W, Brunner J, Rapoport T. The Sec61p Complex Mediates the Integration of a Membrane Protein by Allowing Lipid Partitioning of the Transmembrane Domain. Cell 2000, 102: 233-244. PMID: 10943843, DOI: 10.1016/s0092-8674(00)00028-3.Peer-Reviewed Original Research
1998
Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane
Plath K, Mothes W, Wilkinson B, Stirling C, Rapoport T. Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane. Cell 1998, 94: 795-807. PMID: 9753326, DOI: 10.1016/s0092-8674(00)81738-9.Peer-Reviewed Original ResearchMeSH KeywordsBiological TransportCross-Linking ReagentsEndoplasmic ReticulumFungal ProteinsHSP70 Heat-Shock ProteinsLysineMembrane ProteinsMembrane Transport ProteinsMutagenesisPhenylalaninePhotochemistryProtein Processing, Post-TranslationalProtein Sorting SignalsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsConceptsPosttranslational protein transportSignal sequence recognitionSignal sequenceProtein transportYeast ER membraneProtein-conducting channelYeast endoplasmic reticulumSequence recognitionTransmembrane domain 2Cross-linking studiesATP-independent reactionER membraneCotranslational translocationPolypeptide transportProtein channelsEndoplasmic reticulumDomain 2Membrane componentsSec61pLipid bilayersGeneral mechanismSequenceSec62pKar2pMammalsSignal Sequence Recognition in Cotranslational Translocation by Protein Components of the Endoplasmic Reticulum Membrane
Mothes W, Jungnickel B, Brunner J, Rapoport T. Signal Sequence Recognition in Cotranslational Translocation by Protein Components of the Endoplasmic Reticulum Membrane. Journal Of Cell Biology 1998, 142: 355-364. PMID: 9679136, PMCID: PMC2133054, DOI: 10.1083/jcb.142.2.355.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesBiological Transport, ActiveCross-Linking ReagentsDetergentsDogsEndoplasmic ReticulumFungal ProteinsIn Vitro TechniquesIntracellular MembranesMembrane LipidsMembrane ProteinsProlactinProtein BiosynthesisProtein PrecursorsRibosomesSaccharomyces cerevisiae ProteinsSEC Translocation ChannelsSignal Recognition ParticleSolutionsConceptsEndoplasmic reticulum membraneSignal sequenceProtein componentsReticulum membraneSignal sequence recognitionSequence recognitionProtein-protein interactionsPhotocross-linking experimentsTranslocation channelCotranslational insertionTranslocation componentsCotranslational translocationMembrane proteinsSecretory proteinsNative membranesBinding sitesBulk lipidsSpecific binding sitesProteinDetergent solutionSequenceLipidsMembraneTranslocationSites
1994
Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane.
Mothes W, Prehn S, Rapoport T. Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane. The EMBO Journal 1994, 13: 3973-3982. PMID: 8076593, PMCID: PMC395317, DOI: 10.1002/j.1460-2075.1994.tb06713.x.Peer-Reviewed Original ResearchMeSH KeywordsAffinity LabelsAmino Acid SequenceAzirinesBenzoatesBiological TransportCell CompartmentationCross-Linking ReagentsDNA Mutational AnalysisEndoplasmic ReticulumLysineMembrane ProteinsModels, BiologicalMolecular Sequence DataProlactinProtein BiosynthesisProtein PrecursorsSEC Translocation ChannelsStructure-Activity RelationshipUltraviolet RaysConceptsSec61 alphaNascent chainsProtein interactsSignal sequenceProtein-conducting channelSecretory protein preprolactinNascent polypeptide chainsEndoplasmic reticulum membranePhoto-crosslinking approachSec61p complexER membraneMembrane proteinsMembrane environmentSecretory proteinsPolypeptide segmentsReticulum membranePolypeptide chainTranslocation processHydrophobic coreRibosomesProtein environmentProteinTranslocationPhotoreactive groupSequence