1992
Identification of amino acid residues at the interface of a bacteriophage T4 regA protein-nucleic acid complex.
Webster K, Keill S, Konigsberg W, Williams K, Spicer E. Identification of amino acid residues at the interface of a bacteriophage T4 regA protein-nucleic acid complex. Journal Of Biological Chemistry 1992, 267: 26097-26103. PMID: 1464621, DOI: 10.1016/s0021-9258(18)35722-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBacteriophage T4Base SequenceBinding SitesChromatography, High Pressure LiquidCross-Linking ReagentsMolecular Sequence DataOligoribonucleotidesPeptide FragmentsPlasmidsPromoter Regions, GeneticRNA, MessengerRNA, ViralSequence Homology, Amino AcidTrypsinUltraviolet RaysConceptsCross-linked peptidesProtein-nucleic acid complexesAnion-exchange high-performance liquid chromatographyNucleic acidsIntact proteinHigh-performance liquid chromatographyCross-linked complexGas-phase sequencingPerformance liquid chromatographyAcid complexesExchange high performance liquid chromatographyLiquid chromatographyChemical cleavageBacteriophage T4 regA proteinNucleic acid bindingTryptic peptidesComplexesUltraviolet lightCNBr peptidesPeptidesCN6Amino acid residuesMeasurable affinityAcid bindingAcid
1991
Single‐stranded DNA binding proteins (SSBs) from prokaryotic transmissible plasmids
Ruvolo P, Keating K, Williams K, Chase J. Single‐stranded DNA binding proteins (SSBs) from prokaryotic transmissible plasmids. Proteins Structure Function And Bioinformatics 1991, 9: 120-134. PMID: 2008432, DOI: 10.1002/prot.340090206.Peer-Reviewed Original ResearchConceptsAmino acid residuesSSB proteinDNA bindingE. coli SSB proteinAcid residuesHelix-destabilizing proteinsEscherichia coli SSBAmino acid sequenceNH2-terminal regionCOOH-terminal regionProteins divergeSequence comparisonProtein sequencesSequence homologyAcid sequenceF plasmidPhe-60Trp-40Trp-54NH2-terminalTerminal thirdDNA binding studiesElongation rateTyr-70Protein
1989
The 44P Subunit of the T4 DNA Polymerase Accessory Protein Complex Catalyzes ATP Hydrolysis
Rush J, Lin T, Quinones M, Spicer E, Douglas I, Williams K, Konigsberg W. The 44P Subunit of the T4 DNA Polymerase Accessory Protein Complex Catalyzes ATP Hydrolysis. Journal Of Biological Chemistry 1989, 264: 10943-10953. PMID: 2786875, DOI: 10.1016/s0021-9258(18)60410-7.Peer-Reviewed Original ResearchConceptsAccessory proteinsATP hydrolysisDNA-dependent ATP hydrolysisT4 DNA polymerase accessory proteinsDNA polymerase accessory proteinPolymerase accessory proteinsTotal cellular proteinAccessory protein complexProtein complexesCellular proteinsPlasmid resultsSubunitsProteinATPase activityOverexpression plasmidProductive interactionInduction of cellsPlasmidSpecific activityComplexesSubcomplexInductionGenesOverexpressionATPase
1986
Escherichia coli exonuclease VII. Cloning and sequencing of the gene encoding the large subunit (xseA).
Chase J, Rabin B, Murphy J, Stone K, Williams K. Escherichia coli exonuclease VII. Cloning and sequencing of the gene encoding the large subunit (xseA). Journal Of Biological Chemistry 1986, 261: 14929-14935. PMID: 3021756, DOI: 10.1016/s0021-9258(18)66806-1.Peer-Reviewed Original ResearchConceptsExonuclease VII activityLarge subunitStandard E. coli genetic mapE. coli genetic mapEscherichia coli exonuclease VIIDeletion mutant strainAmino acid sequenceGenetic mapGene productsAcid sequenceMutant strainActive enzymeCell extractsBase pairsGenesExonuclease VIIAmino acidsSubunitsProteinSequenceGuaBXseACloningPromoterMolecular weightMammalian single‐stranded DNA binding protein UP I is derived from the hnRNP core protein A1.
Riva S, Morandi C, Tsoulfas P, Pandolfo M, Biamonti G, Merrill B, Williams K, Multhaup G, Beyreuther K, Werr H. Mammalian single‐stranded DNA binding protein UP I is derived from the hnRNP core protein A1. The EMBO Journal 1986, 5: 2267-2273. PMID: 3023065, PMCID: PMC1167110, DOI: 10.1002/j.1460-2075.1986.tb04494.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntibodiesBase SequenceCattleCell NucleusCross ReactionsDNA HelicasesGenetic VectorsHeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsHumansMolecular WeightPeptide MappingPlasmidsRibonucleoproteinsStructure-Activity RelationshipThymus GlandThymus Hormones
1984
Photochemical cross-linking of the Escherichia coli single-stranded DNA-binding protein to oligodeoxynucleotides. Identification of phenylalanine 60 as the site of cross-linking.
Merrill B, Williams K, Chase J, Konigsberg W. Photochemical cross-linking of the Escherichia coli single-stranded DNA-binding protein to oligodeoxynucleotides. Identification of phenylalanine 60 as the site of cross-linking. Journal Of Biological Chemistry 1984, 259: 10850-10856. PMID: 6540775, DOI: 10.1016/s0021-9258(18)90591-0.Peer-Reviewed Original ResearchConceptsReversed-phase ion-pair high-performance liquid chromatographyIon-pair high-performance liquid chromatographySolid-phase sequence analysisFuture structure/function studiesPeptide-oligonucleotide complexesHigh-performance liquid chromatographyProtein-oligonucleotide complexesLiquid chromatographyPurification procedurePeptide complexesUltraviolet irradiationComplexesStructure/function studiesUltraviolet lightPeptide comprisingCalf thymusGeneral applicabilityAmino acidsChromatographyNucleic acid-binding proteinsReactionThymineExtensive studyIrradiationAcid
1983
F sex factor encodes a single-stranded DNA binding protein (SSB) with extensive sequence homology to Escherichia coli SSB.
Chase J, Merrill B, Williams K. F sex factor encodes a single-stranded DNA binding protein (SSB) with extensive sequence homology to Escherichia coli SSB. Proceedings Of The National Academy Of Sciences Of The United States Of America 1983, 80: 5480-5484. PMID: 6351061, PMCID: PMC384281, DOI: 10.1073/pnas.80.18.5480.Peer-Reviewed Original ResearchConceptsF sex factorE. coli SSBAmino acid residuesE. coli SSB proteinAcid residuesEscherichia coli SSBDNA binding proteinE. coli proteinsShine-Dalgarno sequenceAmino acid sequenceExtensive sequence homologyNH2-terminal regionSex factorSSB proteinEvolutionary significanceColi proteinsDNA replicationPresumptive promoterExtensive homologySequence homologyAcid sequenceDyad symmetryFunctional domainsF plasmidTerminator regionsMolecular cloning of the cDNA coding for rat ornithine transcarbamoylase.
Horwich A, Kraus J, Williams K, Kalousek F, Konigsberg W, Rosenberg L. Molecular cloning of the cDNA coding for rat ornithine transcarbamoylase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1983, 80: 4258-4262. PMID: 6576335, PMCID: PMC384016, DOI: 10.1073/pnas.80.14.4258.Peer-Reviewed Original ResearchConceptsOrnithine transcarbamoylaseSequential Edman analysesCDNA probeMitochondrial matrix enzymeInsertion of cDNAAmino acid residuesConsecutive amino acid residuesCarboxyl-terminal portionCytoplasmic polysomesMolecular cloningCDNA clonesEdman analysisDifferential colony hybridizationTranslation assaysX chromosomeCDNA codingMatrix enzymeEnzyme subunitMessenger speciesAcid residuesSequence presentPolysome immunoadsorptionIdentical subunitsColony hybridizationEscherichia coli