2012
Remote control of DNA-acting enzymes by varying the Brownian dynamics of a distant DNA end
Bai H, Kath J, Zörgiebel F, Sun M, Ghosh P, Hatfull G, Grindley N, Marko J. Remote control of DNA-acting enzymes by varying the Brownian dynamics of a distant DNA end. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 16546-16551. PMID: 23011800, PMCID: PMC3478594, DOI: 10.1073/pnas.1203118109.Peer-Reviewed Original Research
2008
Chemical shift mapping of γδ resolvase dimer and activated tetramer: Mechanistic implications for DNA strand exchange
Gehman J, Cocco M, Grindley N. Chemical shift mapping of γδ resolvase dimer and activated tetramer: Mechanistic implications for DNA strand exchange. Biochimica Et Biophysica Acta 2008, 1784: 2086-2092. PMID: 18840551, DOI: 10.1016/j.bbapap.2008.08.023.Peer-Reviewed Original ResearchConceptsDNA strand exchangeStrand exchangeChemical shift mappingWild-type dimerNMR chemical shift assignmentsChemical shift assignmentsDNA recombinaseResolvase dimersX-ray diffraction modelSequence regionsSubunit interfaceTetrameric stateProtomer-protomer interactionsGammadelta resolvaseShift mappingShift assignmentsMechanistic hypothesesStructural variationsResiduesFingers-Closing and Other Rapid Conformational Changes in DNA Polymerase I (Klenow Fragment) and Their Role in Nucleotide Selectivity
Joyce CM, Potapova O, DeLucia AM, Huang X, Basu VP, Grindley ND. Fingers-Closing and Other Rapid Conformational Changes in DNA Polymerase I (Klenow Fragment) and Their Role in Nucleotide Selectivity. Biochemistry 2008, 47: 6103-6116. PMID: 18473481, DOI: 10.1021/bi7021848.Peer-Reviewed Original Research
2006
Implications of structures of synaptic tetramers of γδ resolvase for the mechanism of recombination
Kamtekar S, Ho RS, Cocco MJ, Li W, Wenwieser SV, Boocock MR, Grindley ND, Steitz TA. Implications of structures of synaptic tetramers of γδ resolvase for the mechanism of recombination. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 10642-10647. PMID: 16807292, PMCID: PMC1483221, DOI: 10.1073/pnas.0604062103.Peer-Reviewed Original ResearchThe Properties of Steric Gate Mutants Reveal Different Constraints within the Active Sites of Y-family and A-family DNA Polymerases*
DeLucia A, Chaudhuri S, Potapova O, Grindley N, Joyce C. The Properties of Steric Gate Mutants Reveal Different Constraints within the Active Sites of Y-family and A-family DNA Polymerases*. Journal Of Biological Chemistry 2006, 281: 27286-27291. PMID: 16831866, DOI: 10.1074/jbc.m604393200.Peer-Reviewed Original ResearchMechanisms of Site-Specific Recombination*
Grindley ND, Whiteson KL, Rice PA. Mechanisms of Site-Specific Recombination*. Annual Review Of Biochemistry 2006, 75: 567-605. PMID: 16756503, DOI: 10.1146/annurev.biochem.73.011303.073908.Peer-Reviewed Original Research
2005
Structure of a Synaptic γδ Resolvase Tetramer Covalently Linked to Two Cleaved DNAs
Li W, Kamtekar S, Xiong Y, Sarkis GJ, Grindley ND, Steitz TA. Structure of a Synaptic γδ Resolvase Tetramer Covalently Linked to Two Cleaved DNAs. Science 2005, 309: 1210-1215. PMID: 15994378, DOI: 10.1126/science.1112064.Peer-Reviewed Original Research
2003
The Architecture of the γδ Resolvase Crossover Site Synaptic Complex Revealed by Using Constrained DNA Substrates
Leschziner A, Grindley N. The Architecture of the γδ Resolvase Crossover Site Synaptic Complex Revealed by Using Constrained DNA Substrates. Molecular Cell 2003, 12: 775-781. PMID: 14527421, DOI: 10.1016/s1097-2765(03)00351-4.Peer-Reviewed Original Research
2001
A Model for the γδ Resolvase Synaptic Complex
Sarkis G, Murley L, Leschziner A, Boocock M, Stark W, Grindley N. A Model for the γδ Resolvase Synaptic Complex. Molecular Cell 2001, 8: 623-631. PMID: 11583624, DOI: 10.1016/s1097-2765(01)00334-3.Peer-Reviewed Original ResearchContacts between the 5′ Nuclease of DNA Polymerase I and Its DNA Substrate*
Xu Y, Potapova O, Leschziner A, Grindley N, Joyce C. Contacts between the 5′ Nuclease of DNA Polymerase I and Its DNA Substrate*. Journal Of Biological Chemistry 2001, 276: 30167-30177. PMID: 11349126, DOI: 10.1074/jbc.m100985200.Peer-Reviewed Original ResearchMeSH KeywordsArginineBase SequenceBinding SitesCircular DichroismDNADNA Polymerase IDNA RepairEscherichia coliKineticsLysineModels, ChemicalModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationOrganophosphorus CompoundsPhosphatesProtein BindingProtein Structure, TertiarySubstrate SpecificityTemperatureTime FactorsConceptsDNA substratesDNA polymerase INuclease domainCleavage siteBasic residuesPolymerase IDuplex DNANuclease cleavagePhosphate ethylation interferenceDNA-binding regionActive site regionDNA replicationOne-half turnBacteriophage T5Eukaryotic nucleasesSubstrate bindingAbasic DNAEthylation interferenceDuplex portionHelical archNucleaseSite regionEscherichia coliMethylphosphonate substitutionsPrimer strand
2000
Coordination between the Polymerase and 5′-Nuclease Components of DNA Polymerase I of Escherichia coli *
Xu Y, Grindley N, Joyce C. Coordination between the Polymerase and 5′-Nuclease Components of DNA Polymerase I of Escherichia coli *. Journal Of Biological Chemistry 2000, 275: 20949-20955. PMID: 10806216, DOI: 10.1074/jbc.m909135199.Peer-Reviewed Original Research
1998
Tn552 transposase catalyzes concerted strand transfer in vitro
Leschziner A, Griffin T, Grindley N. Tn552 transposase catalyzes concerted strand transfer in vitro. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 7345-7350. PMID: 9636151, PMCID: PMC22612, DOI: 10.1073/pnas.95.13.7345.Peer-Reviewed Original Research
1995
A functional analysis of the inverted repeat of the gamma delta transposable element.
May E, Grindley N. A functional analysis of the inverted repeat of the gamma delta transposable element. Journal Of Molecular Biology 1995, 247: 578-87. PMID: 7723015, DOI: 10.1006/jmbi.1995.0164.Peer-Reviewed Original ResearchConceptsIntegration host factorInverted repeatsBase pairsTransposable elementsTransposase bindingGroove contactsIHF siteReduced transposition activityTerminal inverted repeatsMinor groove contactsBase pair regionGamma delta transposaseBase pair stretchSusceptible to mutationsTransposon gamma deltaTn3 familyTransposition activityPoint mutantsTarget plasmidTransposition defectBinding regionMutationsBinding sitesBinding contactsHost factorsA functional analysis of the inverted repeat of the γδ transposable element
May E, Grindley N. A functional analysis of the inverted repeat of the γδ transposable element. Journal Of Molecular Biology 1995, 247: 578-587. DOI: 10.1016/s0022-2836(05)80139-1.Peer-Reviewed Original ResearchThe tyrosine‐6 hydroxyl of γδ resolvase is not required for the DNA cleavage and rejoining reactions
Leschziner A, Boocock M, Grindley N. The tyrosine‐6 hydroxyl of γδ resolvase is not required for the DNA cleavage and rejoining reactions. Molecular Microbiology 1995, 15: 865-870. PMID: 7596288, DOI: 10.1111/j.1365-2958.1995.tb02356.x.Peer-Reviewed Original Research
1993
Mapping interactions between the catalytic domain of resolvase and its DNA substrate using cysteine-coupled EDTA-iron.
Mazzarelli J, Ermácora M, Fox R, Grindley N. Mapping interactions between the catalytic domain of resolvase and its DNA substrate using cysteine-coupled EDTA-iron. Biochemistry 1993, 32: 2979-86. PMID: 8384484, DOI: 10.1021/bi00063a008.Peer-Reviewed Original Research
1992
Reactions at the polymerase active site that contribute to the fidelity of Escherichia coli DNA polymerase I (Klenow fragment).
Joyce C, Sun X, Grindley N. Reactions at the polymerase active site that contribute to the fidelity of Escherichia coli DNA polymerase I (Klenow fragment). Journal Of Biological Chemistry 1992, 267: 24485-24500. PMID: 1447195, DOI: 10.1016/s0021-9258(18)35792-2.Peer-Reviewed Original Research
1991
Resolvase‐catalysed reactions between res sites differing in the central dinucleotide of subsite I.
Stark W, Grindley N, Hatfull G, Boocock M. Resolvase‐catalysed reactions between res sites differing in the central dinucleotide of subsite I. The EMBO Journal 1991, 10: 3541-3548. PMID: 1655422, PMCID: PMC453083, DOI: 10.1002/j.1460-2075.1991.tb04918.x.Peer-Reviewed Original Research
1990
The crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolution
Sanderson M, Freemont P, Rice P, Goldman A, Hatfull G, Grindley N, Steitz T. The crystal structure of the catalytic domain of the site-specific recombination enzyme γδ resolvase at 2.7 Å resolution. Cell 1990, 63: 1323-1329. PMID: 2175678, DOI: 10.1016/0092-8674(90)90427-g.Peer-Reviewed Original ResearchSaturation mutagenesis of the DNA site bound by the small carboxy‐terminal domain of gamma delta resolvase.
Rimphanitchayakit V, Grindley N. Saturation mutagenesis of the DNA site bound by the small carboxy‐terminal domain of gamma delta resolvase. The EMBO Journal 1990, 9: 719-725. PMID: 2155779, PMCID: PMC551726, DOI: 10.1002/j.1460-2075.1990.tb08165.x.Peer-Reviewed Original Research