2018
Subcellular Organization: A Critical Feature of Bacterial Cell Replication
Surovtsev IV, Jacobs-Wagner C. Subcellular Organization: A Critical Feature of Bacterial Cell Replication. Cell 2018, 172: 1271-1293. PMID: 29522747, PMCID: PMC5870143, DOI: 10.1016/j.cell.2018.01.014.Peer-Reviewed Original ResearchConceptsSelf-replicating entitiesCellular lifeStructured genomesDynamic spatial patternsChallenge cellsIntracellular organellesCellular replicationCytoskeletal filamentsBacterial cellsUnique biological propertiesComplex internal organizationSpatial organizationSmall formsCell replicationActive transportLiving systemsBacteriaReplicationGenomeBiological propertiesCellsSpatial patternsOrganellesPowerful meansHallmark
2016
Replication fork passage drives asymmetric dynamics of a critical nucleoid‐associated protein in Caulobacter
Arias‐Cartin R, Dobihal GS, Campos M, Surovtsev IV, Parry B, Jacobs‐Wagner C. Replication fork passage drives asymmetric dynamics of a critical nucleoid‐associated protein in Caulobacter. The EMBO Journal 2016, 36: 301-318. PMID: 28011580, PMCID: PMC5286365, DOI: 10.15252/embj.201695513.Peer-Reviewed Original ResearchConceptsNucleoid-associated proteinsDNA replicationNovel nucleoid-associated proteinGene expressionReplication fork passageGlobal gene expressionCell cycle regulationDNA-binding activityCell cycle progressionChromosome dynamicsFork passageChromosome segregationPleiotropic defectsChromosomal biasCaulobacter crescentusAsymmetric localizationReplication forksCellular functionsCycle regulationGenomic techniquesQuantitative cell imagingCell divisionGapRCycle progressionCell cycle
2014
Evidence for a DNA-relay mechanism in ParABS-mediated chromosome segregation
Lim HC, Surovtsev IV, Beltran BG, Huang F, Bewersdorf J, Jacobs-Wagner C. Evidence for a DNA-relay mechanism in ParABS-mediated chromosome segregation. ELife 2014, 3: e02758. PMID: 24859756, PMCID: PMC4067530, DOI: 10.7554/elife.02758.Peer-Reviewed Original ResearchConceptsChromosome segregationPartition complexParA-like proteinBacterial chromosome segregationDNA-binding activityParABS systemCytoplasmic cargoCaulobacter crescentusDNA regionsBiochemical approachesIntracellular transportTranslocation forceCellular parametersChromosomesTransient tethersCrescentusParABSMajor roleSegregationComplexesMechanismProteinTranslocationConservationBacteria
2010
Spatial organization of the flow of genetic information in bacteria
Montero Llopis P, Jackson AF, Sliusarenko O, Surovtsev I, Heinritz J, Emonet T, Jacobs-Wagner C. Spatial organization of the flow of genetic information in bacteria. Nature 2010, 466: 77-81. PMID: 20562858, PMCID: PMC2896451, DOI: 10.1038/nature09152.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCaulobacter crescentusChaperoninsChromosomes, BacterialDiffusionDNA, BacterialEndoribonucleasesEscherichia coliGene Expression Regulation, BacterialIn Situ Hybridization, FluorescenceLac OperonProtein BiosynthesisRibosomesRNA StabilityRNA TransportRNA, BacterialRNA, MessengerTranscription, GeneticConceptsSites of transcriptionC. crescentusCaulobacter crescentusEukaryotic cellsCellular physiologyMRNA decayMature mRNAMRNA processesRNase EMRNA substratesMRNA localizationGenetic informationGene expressionBacterial cellsEscherichia coliQuantitative fluorescenceCrescentusSitu hybridizationSpatial organizationMRNABacteriaLimited dispersionCellsTranscriptionTranslation
2008
Kinetic Modeling of the Assembly, Dynamic Steady State, and Contraction of the FtsZ Ring in Prokaryotic Cytokinesis
Surovtsev I, Morgan J, Lindahl P. Kinetic Modeling of the Assembly, Dynamic Steady State, and Contraction of the FtsZ Ring in Prokaryotic Cytokinesis. PLOS Computational Biology 2008, 4: e1000102. PMID: 18604268, PMCID: PMC2432035, DOI: 10.1371/journal.pcbi.1000102.Peer-Reviewed Original ResearchConceptsSame chemical modelMonomeric unitsPolymeric ringsRapid assemblyChemical modelProkaryotic cytokinesisMembrane surfaceFree energyUnfavorable processMonomeric FtsZKinetic modelingMechanistic complexityInterfacial reactionRingVivo behaviorDynamic steady stateMonomeric subunitsFtsZ polymerizationHydrolysisReactionRing formsAssembly
2007
Nickel-Dependent Oligomerization of the Alpha Subunit of Acetyl-Coenzyme A Synthase/Carbon Monoxide Dehydrogenase †
Tan X, Kagiampakis I, Surovtsev I, Demeler B, Lindahl P. Nickel-Dependent Oligomerization of the Alpha Subunit of Acetyl-Coenzyme A Synthase/Carbon Monoxide Dehydrogenase †. Biochemistry 2007, 46: 11606-11613. PMID: 17887777, PMCID: PMC2528952, DOI: 10.1021/bi7014663.Peer-Reviewed Original ResearchConceptsAlpha subunitCarbon monoxide dehydrogenaseSynthase/carbon monoxide dehydrogenaseApo-alphaHigh molecular weight speciesMolecular weight speciesRecombinant alpha subunitAcetyl-CoA synthase/carbon monoxide dehydrogenaseWeight speciesOpen conformationSulfur proteinA-clusterConformational changesSubunitsStructural scaffoldOligomerizationFe4S4 clusterSpeciesActive siteConformationDehydrogenaseInterrelated eventsActivationOligomerizesDimers
2006
Mössbauer and EPR Study of Recombinant Acetyl-CoA Synthase from Moorella thermoacetica †
Bramlett M, Stubna A, Tan X, Surovtsev I, Münck E, Lindahl P. Mössbauer and EPR Study of Recombinant Acetyl-CoA Synthase from Moorella thermoacetica †. Biochemistry 2006, 45: 8674-8685. PMID: 16834342, DOI: 10.1021/bi060003+.Peer-Reviewed Original Research