2003
Use of 2-Aminopurine Fluorescence To Examine Conformational Changes during Nucleotide Incorporation by DNA Polymerase I (Klenow Fragment) †
Purohit V, Grindley N, Joyce C. Use of 2-Aminopurine Fluorescence To Examine Conformational Changes during Nucleotide Incorporation by DNA Polymerase I (Klenow Fragment) †. Biochemistry 2003, 42: 10200-10211. PMID: 12939148, DOI: 10.1021/bi0341206.Peer-Reviewed Original ResearchInteraction of DNA Polymerase I (Klenow Fragment) with the Single-Stranded Template beyond the Site of Synthesis †
Turner R, Grindley N, Joyce C. Interaction of DNA Polymerase I (Klenow Fragment) with the Single-Stranded Template beyond the Site of Synthesis †. Biochemistry 2003, 42: 2373-2385. PMID: 12600204, DOI: 10.1021/bi026566c.Peer-Reviewed Original Research
2001
Contacts 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
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 Research
1993
Protein‐protein interactions directing resolvase site‐specific recombination: a structure‐function analysis.
Hughes R, Rice P, Steitz T, Grindley N. Protein‐protein interactions directing resolvase site‐specific recombination: a structure‐function analysis. The EMBO Journal 1993, 12: 1447-1458. PMID: 8385604, PMCID: PMC413356, DOI: 10.1002/j.1460-2075.1993.tb05788.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 Research
1988
Gamma delta transposase and integration host factor bind cooperatively at both ends of gamma delta.
Wiater L, Grindley N. Gamma delta transposase and integration host factor bind cooperatively at both ends of gamma delta. The EMBO Journal 1988, 7: 1907-1911. PMID: 2844529, PMCID: PMC457184, DOI: 10.1002/j.1460-2075.1988.tb03024.x.Peer-Reviewed Original Research
1987
The γδ resolvase induces an unusual DNA structure at the recombinational crossover point
Hatfull G, Noble S, Grindley N. The γδ resolvase induces an unusual DNA structure at the recombinational crossover point. Cell 1987, 49: 103-110. PMID: 3030563, DOI: 10.1016/0092-8674(87)90760-4.Peer-Reviewed Original ResearchContacts between gamma delta resolvase and the gamma delta res site.
Falvey E, Grindley N. Contacts between gamma delta resolvase and the gamma delta res site. The EMBO Journal 1987, 6: 815-821. PMID: 3034611, PMCID: PMC553467, DOI: 10.1002/j.1460-2075.1987.tb04824.x.Peer-Reviewed Original Research
1984
Cleavage of the site-specific recombination protein gamma delta resolvase: the smaller of two fragments binds DNA specifically.
Abdel-Meguid S, Grindley N, Templeton N, Steitz T. Cleavage of the site-specific recombination protein gamma delta resolvase: the smaller of two fragments binds DNA specifically. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 2001-2005. PMID: 6326096, PMCID: PMC345424, DOI: 10.1073/pnas.81.7.2001.Peer-Reviewed Original Research
1981
Transposon-mediated site-specific recombination in vitro: DNA cleavage and protein-DNA linkage at the recombination site
Reed R, Grindley N. Transposon-mediated site-specific recombination in vitro: DNA cleavage and protein-DNA linkage at the recombination site. Cell 1981, 25: 721-728. PMID: 6269756, DOI: 10.1016/0092-8674(81)90179-3.Peer-Reviewed Original ResearchConceptsSite-specific recombinationTransposable element gamma deltaDNA cleavageTnpR genePalindromic sequence 5'Intercistronic regionSequence 5DNA moleculesResolution siteResolvaseSame substrate moleculeRecombination sitesAbsence of Mg2Substrate moleculesGenesSame repliconRecombinationDNACleavageTransposonRes sitesSites
1976
polA6, a mutation affecting the DNA binding capacity of DNA polymerase I
Kelly W, Grindley N. polA6, a mutation affecting the DNA binding capacity of DNA polymerase I. Nucleic Acids Research 1976, 3: 2971-2984. PMID: 12497, PMCID: PMC343145, DOI: 10.1093/nar/3.11.2971.Peer-Reviewed Original Research