1994
Purification and nucleic acid binding properties of a fragment of type C1/C2 heterogeneous nuclear ribonucleoprotein from thymic nuclear extracts.
Amrute S, Abdul-Manan Z, Pandey V, Williams K, Modak M. Purification and nucleic acid binding properties of a fragment of type C1/C2 heterogeneous nuclear ribonucleoprotein from thymic nuclear extracts. Biochemistry 1994, 33: 8282-91. PMID: 7518245, DOI: 10.1021/bi00193a015.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCattleCell NucleusChromatographyChromatography, High Pressure LiquidCross-Linking ReagentsCyanogen BromideDNA, Single-StrandedHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear Ribonucleoprotein Group CHeterogeneous-Nuclear RibonucleoproteinsMolecular Sequence DataOligodeoxyribonucleotidesPeptide FragmentsRibonucleoproteinsRNASpectrometry, FluorescenceThymus GlandUltraviolet RaysConceptsHnRNP proteinsOccluded site sizeHeterogeneous nuclear ribonucleoproteinsNucleic acidsSingle-strand nucleic acidNH2-terminal sequencingEukaryotic RNATight tetramerSDS-polyacrylamide gel electrophoresisApparent molecular weightNuclear ribonucleoproteinNuclear extractsLimited proteolysisMass spectrometric analysisRNAProteinPhenylalanine 19Calf thymusGel electrophoresisAdditional ionic interactionsTerminal deoxynucleotidyl transferaseSite sizeAB formMajor siteCell disruption
1992
Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogaster
Shuai K, Gupta C, Hawley R, Chase J, Stone K, Williams K. Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogaster. Nucleic Acids Research 1992, 20: 1379-1385. PMID: 1313969, PMCID: PMC312186, DOI: 10.1093/nar/20.6.1379.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino AcidsAnimalsChromatography, DEAE-CelluloseChromatography, High Pressure LiquidDNA, Single-StrandedDrosophila melanogasterElectrophoresis, Polyacrylamide GelEndonucleasesExonucleasesHot TemperatureHydrogen-Ion ConcentrationKineticsMolecular Sequence DataMolecular WeightSodium ChlorideSubstrate SpecificityUltracentrifugation
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
1990
Active nucleoprotein filaments of single-stranded binding protein and recA protein on single-stranded DNA have a regular repeating structure
Muniyappa K, Williams K, Chase J, Radding C. Active nucleoprotein filaments of single-stranded binding protein and recA protein on single-stranded DNA have a regular repeating structure. Nucleic Acids Research 1990, 18: 3967-3973. PMID: 2374716, PMCID: PMC331100, DOI: 10.1093/nar/18.13.3967.Peer-Reviewed Original ResearchPurification and functional characterization of adenovirus ts111A DNA-binding protein. Fluorescence studies of protein-nucleic acid binding.
Meyers M, Keating K, Roberts W, Williams K, Chase J, Horwitz M. Purification and functional characterization of adenovirus ts111A DNA-binding protein. Fluorescence studies of protein-nucleic acid binding. Journal Of Biological Chemistry 1990, 265: 5875-5882. PMID: 2318838, DOI: 10.1016/s0021-9258(19)39444-x.Peer-Reviewed Original Research
1989
Site-specific mutagenesis of T4 gene 32: the role of tyrosine residues in protein-nucleic acid interactions.
Shamoo Y, Ghosaini L, Keating K, Williams K, Sturtevant J, Konigsberg W. Site-specific mutagenesis of T4 gene 32: the role of tyrosine residues in protein-nucleic acid interactions. Biochemistry 1989, 28: 7409-17. PMID: 2684276, DOI: 10.1021/bi00444a039.Peer-Reviewed Original ResearchMeSH KeywordsCalorimetry, Differential ScanningCircular DichroismDNA, Single-StrandedDNA, ViralDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelEscherichia coliGene Expression RegulationGenes, ViralMutationNucleic Acid DenaturationPoly dA-dTPoly TProtein DenaturationTemperatureThermodynamicsT-PhagesTrypsinTyrosineViral ProteinsZinc
1988
Thermal denaturation of T4 gene 32 protein: effects of zinc removal and substitution.
Keating K, Ghosaini L, Giedroc D, Williams K, Coleman J, Sturtevant J. Thermal denaturation of T4 gene 32 protein: effects of zinc removal and substitution. Biochemistry 1988, 27: 5240-5. PMID: 3262371, DOI: 10.1021/bi00414a044.Peer-Reviewed Original ResearchPhenylalanines that are conserved among several RNA-binding proteins form part of a nucleic acid-binding pocket in the A1 heterogeneous nuclear ribonucleoprotein.
Merrill B, Stone K, Cobianchi F, Wilson S, Williams K. Phenylalanines that are conserved among several RNA-binding proteins form part of a nucleic acid-binding pocket in the A1 heterogeneous nuclear ribonucleoprotein. Journal Of Biological Chemistry 1988, 263: 3307-3313. PMID: 2830282, DOI: 10.1016/s0021-9258(18)69073-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCarrier ProteinsCattleChromatography, AffinityChromatography, High Pressure LiquidDNA HelicasesDNA, Single-StrandedElectrophoresis, Polyacrylamide GelHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsMolecular Sequence DataNucleic AcidsPeptide FragmentsPhenylalaninePhenylthiohydantoinPhotochemistryPoly TRatsRibonucleoproteinsRNA-Binding ProteinsSerine EndopeptidasesThymus HormonesTrypsinConceptsRNA-binding proteinHeterogeneous nuclear ribonucleoproteinsA1 heterogeneous nuclear ribonucleoproteinNuclear ribonucleoproteinRepeat sequencesPhenylalanine residuesRNA-binding pocketDNA-cellulose chromatographyInternal repeat sequencesStaphylococcus aureus VSequence homologyCovalent adduct formationA1 proteinPrimary structurePartial proteolysisAnalogous positionsAmino acidsTryptic peptidesProteinPolypeptideProteolytic fragmentsRibonucleoproteinFirst experimental evidenceResiduesCellulose chromatographyPhotochemical crosslinking of bacteriophage T4 single‐stranded DNA‐binding protein (gp32) to oligo‐p(dT)8: Identification of phenylalanine‐183 as the site of crosslinking
Shamoo Y, Williams K, Konigsberg W. Photochemical crosslinking of bacteriophage T4 single‐stranded DNA‐binding protein (gp32) to oligo‐p(dT)8: Identification of phenylalanine‐183 as the site of crosslinking. Proteins Structure Function And Bioinformatics 1988, 4: 1-6. PMID: 3186689, DOI: 10.1002/prot.340040103.Peer-Reviewed Original ResearchConceptsCovalent bond formationAnion-exchange high-performance liquid chromatographyHigh-performance liquid chromatographyBond formationGas-phase sequencingLiquid chromatographyPhotochemical crosslinkingPhenylthiohydantoin derivativesSer-GlyTryptic peptidesUltraviolet irradiationTyr-AspUltraviolet lightCrosslinkingSer-AsnHigh affinityCleavage productsGln-ValGlu-SerPeptidesPhotolysisTrypsin cleavage productSingle tryptic peptideChromatographyComplexesMammalian heterogeneous nuclear ribonucleoprotein complex protein A1. Large-scale overproduction in Escherichia coli and cooperative binding to single-stranded nucleic acids.
Cobianchi F, Karpel R, Williams K, Notario V, Wilson S. Mammalian heterogeneous nuclear ribonucleoprotein complex protein A1. Large-scale overproduction in Escherichia coli and cooperative binding to single-stranded nucleic acids. Journal Of Biological Chemistry 1988, 263: 1063-1071. PMID: 2447078, DOI: 10.1016/s0021-9258(19)35461-4.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsBase SequenceCelluloseDNADNA, Single-StrandedEscherichia coliFluorescent DyesHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsMolecular Sequence DataPoly ARecombinant ProteinsRibonucleoproteinsRNAConceptsLarge-scale overproductionNH2-terminal domainTerminal domainDomain peptideCooperative protein-protein interactionsEscherichia coliProtein-induced fluorescence enhancementAmino acidsProtein-protein interactionsNucleic acidsAlpha-helix structureProtein A1Cooperative bindingAssociation constantsSynthetic polypeptide analogueProteinDirect interactionNatural proteinsRecombinant A1Low association constantsBindingIntact A1ColiFluorescence enhancementOverproductionSynthesis of the p10 single-stranded nucleic acid binding protein from murine leukemia virus.
Roberts W, Elliott J, McMurray W, Williams K. Synthesis of the p10 single-stranded nucleic acid binding protein from murine leukemia virus. Chemical Biology & Drug Design 1988, 1: 74-80. PMID: 2856555.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsCircular DichroismCysteineDNA, Single-StrandedDNA-Binding ProteinsGene Products, gagGenes, gagLeukemia Virus, MurineMass SpectrometryPoly AConceptsBeta strandsAlpha-helixDirect amino acid sequencingSynthetic peptide bindsMurine leukemia virus proteinsAmino acid sequencingLys-C peptidesRetroviral Gag polyproteinFasman analysisGene 32Nucleic acidsP10 proteinCircular dichroism experimentsCys-X2Cysteine positionsBacteriophage T4Endoproteinase Lys-C peptidesPrimary sequenceMurine leukemia virusNative proteinPrimary structureCys-X4Amino acid analysisProteinSimilar sequences
1986
Cloning of T4 gene 32 and expression of the wild-type protein under lambda promoter PL regulation in Escherichia coli.
Shamoo Y, Adari H, Konigsberg W, Williams K, Chase J. Cloning of T4 gene 32 and expression of the wild-type protein under lambda promoter PL regulation in Escherichia coli. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 8844-8848. PMID: 2947239, PMCID: PMC387029, DOI: 10.1073/pnas.83.23.8844.Peer-Reviewed Original ResearchConceptsGene 32T4 gene 32Bacteriophage T4 gene 32T4 DNA replicationWild-type proteinWild-type geneHost cell viabilityTranslational regulationCodon TAGDNA replicationNative promoterPromoter PLAutoregulatory regionRich sequencesRestriction fragmentsEscherichia coliTranscriptsCell viabilityProteinRegulationSynthetic oligodeoxynucleotidesDeleterious effectsCloningMutagenesisG32PGene 32 protein, the single-stranded DNA binding protein from bacteriophage T4, is a zinc metalloprotein.
Giedroc D, Keating K, Williams K, Konigsberg W, Coleman J. Gene 32 protein, the single-stranded DNA binding protein from bacteriophage T4, is a zinc metalloprotein. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 8452-8456. PMID: 3490667, PMCID: PMC386948, DOI: 10.1073/pnas.83.22.8452.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCadmiumCobaltDNA, Single-StrandedDNA-Binding ProteinsMetalloproteinsPoly TT-PhagesTrypsinViral ProteinsZincConceptsGene 32 proteinApo-g32PT4-infected Escherichia coliBacteriophage T4-infected Escherichia coliTyrosine-rich sequenceP-hydroxymercuriphenylsulfonatePlasmid pKC30Sequence CysBacteriophage T4Limited proteolysisConformational elementsEscherichia coliProteinDNAEDTA resultsG32PCysteineFragment ASide chainsPKC30ComplexesProteolysisColiSequenceLinear incorporationSingle-Stranded DNA Binding Proteins Required for DNA Replication
Chase J, Williams K. Single-Stranded DNA Binding Proteins Required for DNA Replication. Annual Review Of Biochemistry 1986, 55: 103-136. PMID: 3527040, DOI: 10.1146/annurev.bi.55.070186.000535.Peer-Reviewed Original ResearchProtein chemistry‐nuclear magnetic resonance approach to mapping functional domains in single‐stranded DNA binding proteins
Coleman J, Williams K, King G, Prigodich R, Shamoo Y, Konigsberg W. Protein chemistry‐nuclear magnetic resonance approach to mapping functional domains in single‐stranded DNA binding proteins. Journal Of Cellular Biochemistry 1986, 32: 305-326. PMID: 3543031, DOI: 10.1002/jcb.240320407.Peer-Reviewed Original Research
1985
Amino acid sequence of the UP1 calf thymus helix-destabilizing protein and its homology to an analogous protein from mouse myeloma.
Williams K, Stone K, LoPresti M, Merrill B, Planck S. Amino acid sequence of the UP1 calf thymus helix-destabilizing protein and its homology to an analogous protein from mouse myeloma. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 5666-5670. PMID: 2994041, PMCID: PMC390612, DOI: 10.1073/pnas.82.17.5666.Peer-Reviewed Original ResearchConceptsAmino acid sequenceAmino acidsAnalogous proteinsAcid sequenceHelix-destabilizing proteinsComplete amino acid sequenceHelix-destabilizing proteinStaphylococcus aureus V8 proteaseSimilar amino acidsAureus V8 proteaseMouse proteinCyanogen bromide cleavageMouse sequencesProtein sequencesSequence homologyCOOH terminusNH2 terminusSolid-phase sequencingGas-phase sequencingV8 proteaseEndoproteinase LysTryptic peptidesProteinUP1Calf thymus
1984
Characterization of the Escherichia coli SSB-113 mutant single-stranded DNA-binding protein. Cloning of the gene, DNA and protein sequence analysis, high pressure liquid chromatography peptide mapping, and DNA-binding studies.
Chase J, L'Italien J, Murphy J, Spicer E, Williams K. Characterization of the Escherichia coli SSB-113 mutant single-stranded DNA-binding protein. Cloning of the gene, DNA and protein sequence analysis, high pressure liquid chromatography peptide mapping, and DNA-binding studies. Journal Of Biological Chemistry 1984, 259: 805-814. PMID: 6363409, DOI: 10.1016/s0021-9258(17)43529-0.Peer-Reviewed Original Research
1983
Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins.
Williams K, Spicer E, LoPresti M, Guggenheimer R, Chase J. Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins. Journal Of Biological Chemistry 1983, 258: 3346-3355. PMID: 6298232, DOI: 10.1016/s0021-9258(18)32867-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceDNA HelicasesDNA, Single-StrandedDNA-Binding ProteinsEscherichia coliKineticsMolecular WeightPeptide FragmentsT-PhagesConceptsCOOH terminusBacteriophage T4 gene 32 proteinDNA-induced conformational changesT4 gene 32 proteinConformational changesEscherichia coliHelix-destabilizing proteinGene 32 proteinE. coli DNA replicationSimilar functional domainsCOOH-terminal domainLimited proteolysis studiesEukaryotic DNADNA replicationDouble-helical DNAHomologous domainsTerminal domainFunctional domainsT4 DNAProteolysis studiesLimited proteolysisTerminal regionAmino acidsProteinHelical DNA
1981
DNA helix-destabilizing proteins.
Williams K, Konigsberg W. DNA helix-destabilizing proteins. Gene Amplification And Analysis 1981, 2: 475-508. PMID: 6765652.Peer-Reviewed Original Research