1996
Cis preference of the IS 903 transposase is mediated by a combination of transposase instability and inefficient translation
Derbyshire K, Grindley N. Cis preference of the IS 903 transposase is mediated by a combination of transposase instability and inefficient translation. Molecular Microbiology 1996, 21: 1261-1272. PMID: 8898394, DOI: 10.1111/j.1365-2958.1996.tb02587.x.Peer-Reviewed Original ResearchConceptsClasses of mutationsLevel of transpositionDNA-binding proteinsCis-acting proteinsAmount of transposaseCis preferenceWild-type transposaseInefficient translation initiationSite of synthesisAmino acids 25Translation initiationTranslational initiationTransposase proteinTranslation efficiencyMutant geneGene expressionProtein instabilityTransposase geneInefficient translationProline substitutionTransposaseMutant transposaseMutationsProteinUnusual class
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 factors
1990
Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli.
Polesky A, Steitz T, Grindley N, Joyce C. Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli. Journal Of Biological Chemistry 1990, 265: 14579-14591. PMID: 2201688, DOI: 10.1016/s0021-9258(18)77342-0.Peer-Reviewed Original ResearchConceptsCluster of residuesIdentification of residuesSite-directed mutagenesisActive site residuesAmino acid residuesFuture mutational studiesImportant active site residuesDNA-binding propertiesActive site regionDNA polymerase IGenetic screenPosition 849Polymerase active siteMutant proteinsDNA substratesMutational studiesPolymerase IBiochemical experimentsSite residuesAcid residuesSite regionEscherichia coliPolymerase activityMutationsPolymerase reaction
1985
Genetic mapping and DNA sequence analysis of mutations in the polA gene of Escherichia coli
Joyce C, Fujii D, Laks H, Hughes C, Grindley N. Genetic mapping and DNA sequence analysis of mutations in the polA gene of Escherichia coli. Journal Of Molecular Biology 1985, 186: 283-293. PMID: 3910840, DOI: 10.1016/0022-2836(85)90105-6.Peer-Reviewed Original ResearchConceptsDNA sequence analysisDNA polymerase IThree-dimensional structurePolymerase ISequence analysisPolA geneSingle-subunit enzymeEscherichia coliEnzyme-DNA interactionsGenetic mappingDeletion mutantsSubunit enzymeMutant formsPrimary sequenceMutational changesBacteriophage lambdaExcellent modelPolA mutantsPolA mutationEnzymatic behaviorMutantsMutationsGenesDNAColi
1980
THE PRIMARY STRUCTURE OF DNA POLYMERASE I OF E. COLI11This work was supported by Health and Research Services Foundation grant V-34 (to NDFG), NIH grant GM24688 (to WSK) and ACS Faculty Research Award 198 (to WSK).
Joyce C, Kelley W, Brown W, Grindley N. THE PRIMARY STRUCTURE OF DNA POLYMERASE I OF E. COLI11This work was supported by Health and Research Services Foundation grant V-34 (to NDFG), NIH grant GM24688 (to WSK) and ACS Faculty Research Award 198 (to WSK). 1980, 589-596. DOI: 10.1016/b978-0-12-048850-6.50054-5.Peer-Reviewed Original ResearchDNA polymerase IPolymerase IE. coli polA geneAmino acid sequenceHalf-cystine residuesProteolytic cleavage sitesResidues 342Sequence comparisonDNA polymerase I.DNA sequencesResidue 323Acid sequencePolymerase I.PolA geneNative enzymeCleavage siteAmino acidsSequenceGenesProteinMutationsAllelesEnzymeResiduesTrp
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 ResearchMapping of thepolA locus ofEscherichia coli K12: Orientation of the amino- and carboxy-termini of the cistron
Kelley W, Grindley N. Mapping of thepolA locus ofEscherichia coli K12: Orientation of the amino- and carboxy-termini of the cistron. Molecular Genetics And Genomics 1976, 147: 307-314. PMID: 787765, DOI: 10.1007/bf00582882.Peer-Reviewed Original Research