2011
tRNA import into mitochondria: many organisms but not so many mechanisms
Alfonzo J, Randau L, Söll D. tRNA import into mitochondria: many organisms but not so many mechanisms. The FASEB Journal 2011, 25: 311.3-311.3. DOI: 10.1096/fasebj.25.1_supplement.311.3.Peer-Reviewed Original ResearchTRNA importMitochondrial genomeMammalian mitochondriaImport of tRNAsMajority of eukaryotesMitochondrial tRNA mutationsProtein importImport pathwayTRNA genesImport systemAdditional tRNAsTRNA mutationsTRNACellular ATPMitochondriaEukaryotesOrganismsGenomeRat liver mitochondriaLiver mitochondriaImportInnate abilityGenesTrypanosomesCytoplasm
2004
Vpx proteins of SIVmac239 and HIV-2ROD interact with the cytoskeletal protein α-actinin 1
Mueller S, Jung R, Weiler S, Lang S. Vpx proteins of SIVmac239 and HIV-2ROD interact with the cytoskeletal protein α-actinin 1. Journal Of General Virology 2004, 85: 3291-3303. PMID: 15483243, DOI: 10.1099/vir.0.80198-0.Peer-Reviewed Original ResearchMeSH KeywordsActininAmino Acid SequenceAnimalsBiological TransportChlorocebus aethiopsCOS CellsCytoplasmHIV-2Molecular Sequence DataProlineProtein Structure, TertiaryRetroviridae ProteinsSequence AlignmentSimian immunodeficiency virusTransfectionTwo-Hybrid System TechniquesViral Regulatory and Accessory ProteinsConceptsPre-integration complexNuclear localization signalNuclear importProline-rich C-terminal domainClassical import pathwayEfficient nuclear importTwo-hybrid screenAlpha-actinin 1Α-actinin 1C-terminal domainLoss of interactionImport pathwayLocalization signalCellular proteinsNuclear localizationSequence elementsCytoskeletal proteinsVpx geneVpx proteinsQuiescent cellsAA proteinViral proteinsProteinVirion particlesRed-capped mangabeysTransportins 1 and 2 are redundant nuclear import factors for hnRNP A1 and HuR
Rebane A, Aab A, Steitz JA. Transportins 1 and 2 are redundant nuclear import factors for hnRNP A1 and HuR. RNA 2004, 10: 590-599. PMID: 15037768, PMCID: PMC1370549, DOI: 10.1261/rna.5224304.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAmino Acid SequenceAntigens, Surfacebeta KaryopherinsCell NucleusELAV ProteinsELAV-Like Protein 1HeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHumansMolecular Sequence DataMutationProtein Structure, Tertiaryran GTP-Binding ProteinReceptors, Cytoplasmic and NuclearRNA-Binding ProteinsSequence Analysis, ProteinConceptsHnRNP A1Transportin-1Import factorsDigitonin-permeabilized HeLa cellsNuclear import factorsMRNA-binding proteinRecombinant hnRNP A1Binding of HuRImp betaImport pathwayCargo specificityNuclear importExport receptorTransportin-2TransportinTransport signalHeLa cellsLikely actsHuRTrn1ProteinInteraction studiesImportTRN2RanGTP
1998
Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121
Kaffman A, Rank N, O’Shea E. Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121. Genes & Development 1998, 12: 2673-2683. PMID: 9732266, PMCID: PMC317126, DOI: 10.1101/gad.12.17.2673.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCell NucleusCloning, MolecularCytoplasmDNA-Binding ProteinsEscherichia coliFungal ProteinsKineticsMembrane Transport ProteinsPhosphatesPhosphorylationReceptors, Cytoplasmic and NuclearRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factors
1996
Export of Proteins from Mitochondria
Poyton R, Sevarino K, McKee E, Duhl D, Cameron V, Goehring B. Export of Proteins from Mitochondria. Advances In Molecular And Cell Biology 1996, 17: 247-280. DOI: 10.1016/s1569-2558(09)60017-5.Peer-Reviewed Original ResearchNuclear gene productsGene productsIntermembrane spaceInner membraneMitochondrial matrixMembrane coExport of proteinsInner membrane spaceConservative sortingImport pathwayProtein exportLeader peptideLines of evidenceMembrane spaceCytosolProteinMitochondriaPathwayTransport pathwaysPreproteinsMembraneDirect evidenceYeastExportProtease
1991
Protein folding causes an arrest of preprotein translocation into mitochondria in vivo.
Wienhues U, Becker K, Schleyer M, Guiard B, Tropschug M, Horwich A, Pfanner N, Neupert W. Protein folding causes an arrest of preprotein translocation into mitochondria in vivo. Journal Of Cell Biology 1991, 115: 1601-1609. PMID: 1757464, PMCID: PMC2289212, DOI: 10.1083/jcb.115.6.1601.Peer-Reviewed Original ResearchMeSH KeywordsAminopterinBiological TransportIntracellular MembranesKineticsL-Lactate DehydrogenaseL-Lactate Dehydrogenase (Cytochrome)Membrane PotentialsMitochondriaProtein ConformationProtein PrecursorsProtein Processing, Post-TranslationalRecombinant Fusion ProteinsSaccharomyces cerevisiaeTetrahydrofolate DehydrogenaseConceptsMitochondrial protein uptakeTranslocation contact sitesAmino-terminal thirdStable tertiary structureDihydrofolate reductase domainImport pathwayPreprotein translocationHybrid proteinProtein foldingMitochondrial membraneTranslocation sitesContact sitesCytochrome b2Fusion proteinPolypeptide segmentsYeast cellsReductase domainTertiary structureProtein uptakeDihydrofolate reductaseProteinMitochondriaMembraneVivoFoldingMitochondrial protein import.
Horwich A, Cheng M, West A, Pollock R. Mitochondrial protein import. Current Topics In Microbiology And Immunology 1991, 170: 1-42. PMID: 1760928, DOI: 10.1007/978-3-642-76389-2_1.Peer-Reviewed Original ResearchConceptsMitochondrial protein import pathwayProtein import pathwayPrecise molecular functionConformational alterationsImport pathwayMolecular functionsStep of recognitionMembrane translocationProteolytic cleavageProteinTranslocationDynamic picturePowerful toolGeneticsAlterationsPathwayBiochemistryCleavageCritical features
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