2009
Conformational transitions in DNA polymerase I revealed by single-molecule FRET
Santoso Y, Joyce CM, Potapova O, Le Reste L, Hohlbein J, Torella JP, Grindley ND, Kapanidis AN. Conformational transitions in DNA polymerase I revealed by single-molecule FRET. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 107: 715-720. PMID: 20080740, PMCID: PMC2818957, DOI: 10.1073/pnas.0910909107.Peer-Reviewed Original ResearchConceptsDNA polymerase IClosed conformationPolymerase IConformational transitionSingle-molecule fluorescence resonance energy transferEarly stepsSingle-molecule FRETFluorescence resonance energy transferAvailable crystallographic structuresResonance energy transferMost DNA polymerasesComplementary ribonucleotidesChemical stepIncorrect substratesPolymerase moleculesPol DNAReaction pathwaysAcceptor fluorophoresKinetic checkpointsConformational dynamicsConformational flexibilityNucleotide additionStructural studiesDNA polymeraseCrystallographic structure
1997
Two abundant intramolecular transposition products, resulting from reactions initiated at a single end, suggest that IS2 transposes by an unconventional pathway
Lewis L, Grindley N. Two abundant intramolecular transposition products, resulting from reactions initiated at a single end, suggest that IS2 transposes by an unconventional pathway. Molecular Microbiology 1997, 25: 517-529. PMID: 9302014, DOI: 10.1046/j.1365-2958.1997.4871848.x.Peer-Reviewed Original ResearchBacterial ProteinsBase SequenceBinding SitesCloning, MolecularDNA NucleotidyltransferasesDNA PrimersDNA Transposable ElementsDNA, BacterialDNA, CircularEscherichia coliEscherichia coli ProteinsMicroscopy, ElectronModels, GeneticMolecular Sequence DataNucleic Acid ConformationPolymerase Chain ReactionRecombinant Fusion ProteinsTransposases