2024
Cotranslational molecular condensation of cochaperones and assembly factors facilitates axonemal dynein biogenesis
Li Y, Xu W, Cheng Y, Djenoune L, Zhuang C, Cox A, Britto C, Yuan S, Wang S, Sun Z. Cotranslational molecular condensation of cochaperones and assembly factors facilitates axonemal dynein biogenesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2402818121. PMID: 39541357, PMCID: PMC11588059, DOI: 10.1073/pnas.2402818121.Peer-Reviewed Original ResearchConceptsDynein axonemal assembly factorsAssembly factorsCytosolic fociOuter dynein armsMacromolecular machinesAxonemal dyneinsAssembly hubDynein armsMolecular condensateLiquid-liquid phase separationCochaperoneEncoding mRNAFoci formationCiliary motilityStable interactionLRRC6Functional significanceRUVBL1DyneinMRNAAssembly of multiple componentsAssemblyPotential mechanismsRUVBL2Biogenesis
2022
Human pre-60S assembly factors link rRNA transcription to pre-rRNA processing
McCool M, Buhagiar A, Bryant C, Ogawa L, Abriola L, Surovtseva Y, Baserga S. Human pre-60S assembly factors link rRNA transcription to pre-rRNA processing. RNA 2022, 29: rna.079149.122. PMID: 36323459, PMCID: PMC9808572, DOI: 10.1261/rna.079149.122.Peer-Reviewed Original ResearchRRNA transcriptionRRNA processingRibosomal subunit biogenesisRNA polymerase IRibosome biosynthesisSubunit biogenesisRibosome biogenesisRibosome assemblyAssembly factorsTranscription controlBiogenesis factorsRRNA productionSteady-state levelsRNA transcriptionPolymerase IComplex membersHuman cellsProtein synthesisP53 stabilizationTranscriptionEssential processBiogenesisCell proliferationDual roleRegulatory detailsThe flagellar motor protein FliL forms a scaffold of circumferentially positioned rings required for stator activation
Tachiyama S, Chan KL, Liu X, Hathroubi S, Li W, Peterson B, Khan M, Ottemann K, Liu J, Roujeinikova A. The flagellar motor protein FliL forms a scaffold of circumferentially positioned rings required for stator activation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2118401119. PMID: 35046042, PMCID: PMC8794807, DOI: 10.1073/pnas.2118401119.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial Physiological PhenomenaBacterial ProteinsFlagellaHelicobacter pyloriMembrane ProteinsModels, MolecularMolecular Motor ProteinsMultiprotein ComplexesProtein BindingProtein ConformationProtein Interaction Domains and MotifsProtein TransportStructure-Activity RelationshipConceptsStator unitsStomatin/prohibitin/flotillin/HflK/C (SPFH) domainWild-type cellsSignificant structural similarityPeriplasmic domainAssembly factorsFlagellar motorAccessory proteinsFliLLinker regionActive conformationFlagellar baseC-domainMotBStructural similarityStator assemblyProteinPutative mechanismsElectron tomography reconstructionsIntact motorCellsActivationDomainMotAHelix
2019
FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia
Lin J, Le TV, Augspurger K, Tritschler D, Bower R, Fu G, Perrone C, O’Toole E, Mills KV, Dymek E, Smith E, Nicastro D, Porter ME. FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia. Molecular Biology Of The Cell 2019, 30: 2659-2680. PMID: 31483737, PMCID: PMC6761771, DOI: 10.1091/mbc.e19-07-0367.Peer-Reviewed Original ResearchConceptsInner dynein armsRegulatory complexCryo-electron tomographyInner arm dyneinsCiliary motilityMultiple dynein motorsPrecise spatial organizationAxonemal repeatDocking factorUnique binding siteWD repeatsDynein assemblyAssembly factorsDomain proteinsRegulatory hubDynein complexDynein isoformsDynein subunitsInsertional mutagenesisNew lociRegulatory proteinsDynein motorsDifferent dyneinsDoublet microtubulesTransport factors
2017
Axonemal dynein assembly requires the R2TP complex component Pontin
Li Y, Zhao L, Yuan S, Zhang J, Sun Z. Axonemal dynein assembly requires the R2TP complex component Pontin. Development 2017, 144: 4684-4693. PMID: 29113992, PMCID: PMC5769618, DOI: 10.1242/dev.152314.Peer-Reviewed Original ResearchConceptsDynein arm assemblyCilia motilityTah1-Pih1 (R2TP) complexAxonemal dynein assemblyMacromolecular protein complexesIntermediate chain 1Reptin functionsRUVBL1-RUVBL2R2TP complexAAA ATPasesCytosolic punctaArm assemblyDynein assemblyAssembly factorsCytosolic fociProtein complexesZebrafish embryosCilia defectsInner dynein armsPontinCiliated tissuesMouse testisReptinChain 1Dynein arms
2016
Nop9 is a PUF-like protein that prevents premature cleavage to correctly process pre-18S rRNA
Zhang J, McCann KL, Qiu C, Gonzalez LE, Baserga SJ, Hall TM. Nop9 is a PUF-like protein that prevents premature cleavage to correctly process pre-18S rRNA. Nature Communications 2016, 7: 13085. PMID: 27725644, PMCID: PMC5062617, DOI: 10.1038/ncomms13085.Peer-Reviewed Original ResearchConceptsEukaryotic ribosome biogenesisCorrect subcellular locationRibosome assembly factorsPre-ribosomal RNAPumilio repeatsRibosome biogenesisHuman ribosomopathiesAssembly factorsBiogenesis factorsRepeat proteinsMature rRNASubcellular locationNop9RNA complexCleavage siteRRNATimely cleavageProteinStructural featuresFinal processing stepRibosomopathiesBiogenesisCleavageYeastNuclease
2011
Assembly factors as a new class of disease genes for mitochondrial complex I deficiency: cause, pathology and treatment options
Nouws J, Nijtmans L, Smeitink J, Vogel R. Assembly factors as a new class of disease genes for mitochondrial complex I deficiency: cause, pathology and treatment options. Brain 2011, 135: 12-22. PMID: 22036961, DOI: 10.1093/brain/awr261.Peer-Reviewed Original ResearchConceptsComplex I deficiencyAssembly factorsDisease genesI deficiencySpecific assembly factorsGeneral molecular mechanismMitochondrial complex I deficiencyOxidative phosphorylation disordersDisease-causing mutationsSuch genesMolecular mechanismsComplex IGenesLarge diversityProgressive encephalomyopathyChaperonesDiversityMutationsEncephalomyopathyDeficiencyNew class
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