2000
Identification of Genes Encoding Exported Mycobacterium tuberculosis Proteins Using a Tn552′phoA In Vitro Transposition System
Braunstein M, Griffin T, Kriakov J, Friedman S, Grindley N, Jacobs W. Identification of Genes Encoding Exported Mycobacterium tuberculosis Proteins Using a Tn552′phoA In Vitro Transposition System. Journal Of Bacteriology 2000, 182: 2732-2740. PMID: 10781540, PMCID: PMC101980, DOI: 10.1128/jb.182.10.2732-2740.2000.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAmino Acid SequenceArtificial Gene FusionBacterial ProteinsBiological TransportCosmidsCyclin-Dependent KinasesDNA Transposable ElementsDNA, BacterialGenes, BacterialGenomic LibraryMolecular Sequence DataMutagenesis, InsertionalMycobacterium tuberculosisPlasmidsReplication OriginConceptsProtective immunityM. tuberculosisMycobacterium tuberculosis pathogenesisImmune responseTuberculosis pathogenesisMycobacterium tuberculosis proteinsM. tuberculosis databaseTuberculosisTuberculosis databasePathogenesisTuberculosis proteinsImmunityEnvelope-associated proteinsM. smegmatisProteinPeptides
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
1992
Binding of the IS903 transposase to its inverted repeat in vitro.
Derbyshire K, Grindley N. Binding of the IS903 transposase to its inverted repeat in vitro. The EMBO Journal 1992, 11: 3449-3455. PMID: 1324175, PMCID: PMC556880, DOI: 10.1002/j.1460-2075.1992.tb05424.x.Peer-Reviewed Original Research
1991
The Study of Protein-DNA Contacts by Ethylation Interference
Rimphanitchayakit V, Grindley N. The Study of Protein-DNA Contacts by Ethylation Interference. Biomethods 1991, 111-120. DOI: 10.1007/978-3-0348-7561-5_9.Peer-Reviewed Original Research
1990
Cooperativity mutants of the γδ resolvase identify an essential interdimer interaction
Hughes R, Hatfull G, Rice P, Steitz T, Grindley N. Cooperativity mutants of the γδ resolvase identify an essential interdimer interaction. Cell 1990, 63: 1331-1338. PMID: 2175679, DOI: 10.1016/0092-8674(90)90428-h.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsHigher-order protein-protein interactionsCooperativity mutantsSite-specific recombinaseGamma delta resolvaseMutant phenotypeResolvase mutantsNucleoprotein complexesCrystallographic tetramersResolvase dimersΓδ resolvaseResolvaseCooperative bindingMutantsDNARecombinationSide chainsRecombinaseProteinInteractionCointegrate intermediatePhenotypeRecombination reactionBindingTetramerRole of instability in the cis action of the insertion sequence IS903 transposase.
Derbyshire K, Kramer M, Grindley N. Role of instability in the cis action of the insertion sequence IS903 transposase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 4048-4052. PMID: 2161528, PMCID: PMC54044, DOI: 10.1073/pnas.87.11.4048.Peer-Reviewed Original ResearchConceptsDNA-binding proteinsCis actionCis-acting proteinsKilobase of DNAInsertion sequenceGalactosidase fusion proteinWild-type transposaseProtease-deficient strainSite of synthesisLon geneBacterial insertion sequencesUnstable proteinTransposase geneFusion proteinTrans actionTransposaseEscherichia coliProteinDefective transposonTransposonGenes
1986
Analysis of gamma delta resolvase mutants in vitro: evidence for an interaction between serine-10 of resolvase and site I of res.
Hatfull G, Grindley N. Analysis of gamma delta resolvase mutants in vitro: evidence for an interaction between serine-10 of resolvase and site I of res. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 5429-5433. PMID: 3016704, PMCID: PMC386300, DOI: 10.1073/pnas.83.15.5429.Peer-Reviewed Original ResearchConceptsSerine 10Resolvase mutantsRecombinational activitySite-specific recombination proteinsProtein-DNA complexesPosition 10Site-specific recombinationRecombination proteinsActive site serineMutant proteinsRecombinational crossover pointMutantsResolvaseRecombinational sitesLeucine changeSerineSite ICysteine changeGel electrophoresisSpecific defectsComplex formationCointegrate moleculeTransposon gamma deltaProteinDNA
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