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
2004
Exchange of DNA Base Pairs that Coincides with Recognition of Homology Promoted by E. coli RecA Protein
Folta-Stogniew E, O'Malley S, Gupta R, Anderson KS, Radding CM. Exchange of DNA Base Pairs that Coincides with Recognition of Homology Promoted by E. coli RecA Protein. Molecular Cell 2004, 15: 965-975. PMID: 15383285, DOI: 10.1016/j.molcel.2004.08.017.Peer-Reviewed Original ResearchMeSH KeywordsBase CompositionBase PairingBase SequenceDNA, BacterialDNA, Single-StrandedEscherichia coli ProteinsKineticsRec A RecombinasesSequence Homology, Nucleic AcidConceptsE. coli RecA proteinRecognition of homologyColi RecA proteinRecA proteinBase pairsStrand exchangeSynaptic complexDouble-strand breaksT base pairsStopped-flow fluorescenceGenetic recombinationSingle strandsHomologyUnresolved mechanismDuplex DNADNA base pairsDNARate of exchangeProteinDynamic structureComplexesStrandsBasis exchangeRate of formationMechanism