2013
Oligomerization and higher‐order assembly contribute to sub‐cellular localization of a bacterial scaffold
Bowman GR, Perez AM, Ptacin JL, Ighodaro E, Folta‐Stogniew E, Comolli LR, Shapiro L. Oligomerization and higher‐order assembly contribute to sub‐cellular localization of a bacterial scaffold. Molecular Microbiology 2013, 90: 776-795. PMID: 24102805, PMCID: PMC3859194, DOI: 10.1111/mmi.12398.Peer-Reviewed Original ResearchConceptsSub-cellular localizationAmino acidsN-terminal 23 amino acidsDefective mutant proteinsAsymmetric cell divisionC-terminal 76 amino acidsC-terminal domainDimer of trimersCaulobacter crescentusCell polesLocalization determinantsHigher-order structureMutant proteinsScaffold proteinSubcellular fociCell divisionLinker domainPopZMutational analysisBiophysical analysisWild typePolar organizationOrganizing centerDistinct setsProtein
2008
Reexamination of the Role of the Amino Terminus of SecA in Promoting Its Dimerization and Functional State
Das S, Stivison E, Folta-Stogniew E, Oliver D. Reexamination of the Role of the Amino Terminus of SecA in Promoting Its Dimerization and Functional State. Journal Of Bacteriology 2008, 190: 7302-7307. PMID: 18723626, PMCID: PMC2580686, DOI: 10.1128/jb.00593-08.Peer-Reviewed Original ResearchConceptsWild-type SecAProtein-conducting channelCell growthAmino-terminal regionSecA dimerSecA functionsProtein translocationSecA expressionMembrane associationMutant proteinsCell fractionationATPase specific activityCorresponding proteinProtein cargoCarboxyl terminusAmino terminusVivo functionSecADimerization defectFunctional stateMutantsBiochemical studiesResidue resultsProteinChemical cross