1995
Multiple RNA binding domains (RBDs) just don't add up
Shamoo Y, Abdul-Manan N, Williams K. Multiple RNA binding domains (RBDs) just don't add up. Nucleic Acids Research 1995, 23: 725-728. PMID: 7535921, PMCID: PMC306750, DOI: 10.1093/nar/23.5.725.Peer-Reviewed Original ResearchMutagenesis of the COOH-terminal Region of Bacteriophage T4 regA Protein (∗)
O'Malley S, Sattar A, Williams K, Spicer E. Mutagenesis of the COOH-terminal Region of Bacteriophage T4 regA Protein (∗). Journal Of Biological Chemistry 1995, 270: 5107-5114. PMID: 7890619, DOI: 10.1074/jbc.270.10.5107.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBacteriophage T4Base SequenceBinding SitesChymotrypsinCircular DichroismCloning, MolecularDNA PrimersGenes, ViralKineticsMolecular Sequence DataMutagenesis, Site-DirectedPeptide FragmentsPoly UProtein ConformationRecombinant ProteinsSequence DeletionTranscription FactorsConceptsBacteriophage T4 regA proteinRegA proteinPhe-106Deletion mutantsWild-type regA proteinAmino acid substitutionsCOOH-terminal regionSpecific RNA ligandsT4 proteinsTranslational repressorRNA ligandsPartial proteolysisAcid substitutionsMutantsAmino acidsProteinRNAMajor siteNucleic acidsProteolysisOverall free energyChymotryptic cleavageSpecific targetsDomain structureAffinity
1992
Shuffling of amino acid sequence: an important control in synthetic peptide studies of nucleic acid-binding domains. Binding properties of fragments of a conserved eukaryotic RNA binding motif.
Nadler S, Kapouch J, Elliott J, Williams K. Shuffling of amino acid sequence: an important control in synthetic peptide studies of nucleic acid-binding domains. Binding properties of fragments of a conserved eukaryotic RNA binding motif. Journal Of Biological Chemistry 1992, 267: 3750-3757. PMID: 1740426, DOI: 10.1016/s0021-9258(19)50589-0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCarrier ProteinsCircular DichroismFungal ProteinsGenes, FungalHot TemperatureMolecular Sequence DataNucleic Acid DenaturationNucleic AcidsPeptide FragmentsPoly APoly A-UPoly(A)-Binding ProteinsRNA-Binding ProteinsRNA, FungalSaccharomyces cerevisiaeSpectrometry, FluorescenceSubstrate SpecificityConceptsNucleic acidsPeptide studiesResidue peptideSynthetic peptide studiesSynthetic peptidesSynthetic peptide analoguesFree energyProperties of fragmentsPeptide analoguesNucleic acid-binding domainParent proteinLatter peptideNucleic acid bindingAmino acidsStructure/function studiesAmino acid sequenceSignificant affinityAcidEukaryotic RNAPeptidesRNA specificityAmino acid compositionSimilar RNACarboxyl halfMolecular basis
1990
Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain.
Kumar A, Widen S, Williams K, Kedar P, Karpel R, Wilson S. Studies of the domain structure of mammalian DNA polymerase beta. Identification of a discrete template binding domain. Journal Of Biological Chemistry 1990, 265: 2124-2131. PMID: 2404980, DOI: 10.1016/s0021-9258(19)39949-1.Peer-Reviewed Original ResearchConceptsNH2-terminal domainDNA polymerase betaLarge-scale overproductionPolymerase betaMammalian DNA polymerase betaCOOH-terminal domainProtease-sensitive regionNucleic acidsProteolysis experimentsRat proteinRecombinant proteinsPolypeptide chainDNA polymerase activityIntact proteinEscherichia coliAmino acidsTryptic peptidesDNA polymeraseDomain structureProteinPolymerase activityDomainPolymeraseAcidDNA
1989
Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles
Merrill B, Barnett S, LeStourgeon W, Williams K. Primary structure differences between proteins C1 and C2 of HeLa 40S nuclear ribonucleoprotein particles. Nucleic Acids Research 1989, 17: 8441-8449. PMID: 2587210, PMCID: PMC335017, DOI: 10.1093/nar/17.21.8441.Peer-Reviewed Original ResearchConceptsInsert sequenceHeterogeneous nuclear ribonucleoprotein particleSingle transcription unitAlternative splicing mechanismNuclear ribonucleoprotein particleAmino acid sequencingResidue insertHnRNP proteinsTranscription unitTryptic peptide mappingSplicing mechanismPrimary structure differencesC2 proteinSDS-polyacrylamide gel electrophoresisNuclear ribonucleoproteinProtein C1Ribonucleoprotein particleUntranslated regionPrimary structurePolyacrylamide gel electrophoresisAmino acidsPeptide mappingGel electrophoresisMolecular weight differencesProtein
1988
Phenylalanines 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 chromatographyMammalian 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 enhancementOverproduction
1987
Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: identification of histidine-881 as the site of cross-linking.
Pandey V, Williams K, Stone K, Modak M. Photoaffinity labeling of the thymidine triphosphate binding domain in Escherichia coli DNA polymerase I: identification of histidine-881 as the site of cross-linking. Biochemistry 1987, 26: 7744-8. PMID: 3322406, DOI: 10.1021/bi00398a031.Peer-Reviewed Original ResearchConceptsCross-linking reactionReversed-phase high-performance liquid chromatographyHigh-performance liquid chromatographyCross-linking sitesEscherichia coli DNA polymerase IPeptide lossKlenow fragmentChelate formLiquid chromatographyAmino acid analysisE. coli DNA Pol ISmall peptidesTryptic digestionSubstrate deoxynucleoside triphosphateHistidine residuesTryptic peptidesAmino acidsSingle peptideOptimal conditionsPeptide mappingDNA Pol IStaphylococcus aureus V8 protease digestionDNA polymerase IAcceptor sitesPeptidesUse of HPLC Comparative Peptide Mapping in Structure/Function Studies
Williams K, Stone K, Fritz M, Merrill B, Konigsberg W, Pandolfo M, Valentini O, Riva S, Reddigari S, Patel G, Chase J. Use of HPLC Comparative Peptide Mapping in Structure/Function Studies. 1987, 45-52. DOI: 10.1007/978-1-4613-1787-6_5.Peer-Reviewed Original ResearchComparative peptide mappingPeptide mappingActive site peptideGroup-specific reagentsStructure/function studiesGas-phase sequencingProtein structureChemical modificationActive siteCovalent crosslinkingEnzymatic digestsReversed-phase HPLCSite peptideRetention timeSpecific reagentsPhase sequencingHPLCStructureBaseline artifactsIndividual amino acidsLigandsSpecific applicationsPeptidesReagentsAmino acids
1986
Coding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase.
Kraus J, Firgaira F, Novotný J, Kalousek F, Williams K, Williamson C, Ohura T, Rosenberg L. Coding sequence of the precursor of the beta subunit of rat propionyl-CoA carboxylase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 8049-8053. PMID: 3464942, PMCID: PMC386864, DOI: 10.1073/pnas.83.21.8049.Peer-Reviewed Original ResearchConceptsPropionyl-CoA carboxylaseNH2-terminal leader peptideAmino acid sequenceBeta subunitBeta-subunit precursorMature subunitAcid sequenceLeader peptideMitochondrial enzyme propionyl-CoA carboxylaseAmino acidsSubunit precursorOpen reading frameAlpha-helical segmentsEnzyme propionyl-CoA carboxylaseCarboxylaseNH2-terminal residuesFirst helixReading frameDNA sequencesPrecursorsCytoplasmic precursorMRNA sequencesArginine residuesHydrophobic momentMRNA transcriptsEscherichia 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 HormonesPurification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins.
Kumar A, Williams K, Szer W. Purification and domain structure of core hnRNP proteins A1 and A2 and their relationship to single-stranded DNA-binding proteins. Journal Of Biological Chemistry 1986, 261: 11266-11273. PMID: 3733753, DOI: 10.1016/s0021-9258(18)67378-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceChromatography, High Pressure LiquidCircular DichroismDNA-Binding ProteinsHeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsHumansMolecular WeightRibonucleoproteinsSpectrophotometry, UltravioletTrypsinConceptsHeterogeneous nuclear ribonucleoproteinsNucleic acid-binding domainProtein A1Glycine-rich proteinSsDNA-binding proteinDNA-binding proteinsHnRNP protein A1Helix-destabilizing activityHnRNP proteinsNuclear ribonucleoproteinTerminal domainHDP-1A1 bindsGlycine residueNative proteinPrimary structureLimited proteolysisHeLa cellsProtein A2Amino acidsProtein
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 thymusCloning, nucleotide sequence, and overexpression of the bacteriophage T4 regA gene.
Adari H, Rose K, Williams K, Konigsberg W, Lin T, Spicer E. Cloning, nucleotide sequence, and overexpression of the bacteriophage T4 regA gene. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 1901-1905. PMID: 3872458, PMCID: PMC397441, DOI: 10.1073/pnas.82.7.1901.Peer-Reviewed Original ResearchConceptsRegA proteinRegA geneNucleotide sequenceProtein chemical studiesLevel of translationCorresponding genesStructural geneGene codesDNA sequencesRegulatory proteinsAcid inductionDNA fragmentsPhage M13Early genesGenesRestriction fragmentsAmino acidsProteinPAS1Same plasmidSequenceFragmentsCloningRegATranslationA cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites
Kraus J, Hodges P, Williamson C, Horwich A, Kalousek F, Williams K, Rosenberg L. A cDNA clone for the precursor of rat mitochondrial ornithine transcarbamylase: comparison of rat and human leader sequences and conservation of catalytic sites. Nucleic Acids Research 1985, 13: 943-952. PMID: 3839075, PMCID: PMC341044, DOI: 10.1093/nar/13.3.943.Peer-Reviewed Original ResearchConceptsAmino acid sequenceLeader sequenceAcid sequenceBasic residuesAmino-terminal leader sequenceE. coliComplete sequence homologyAmino acid residuesProtein sequence dataOrnithine transcarbamylaseCDNA clonesSequence dataDNA complementaryOrnithine transcarbamylasesSequence homologyEntire proteinHuman enzymeAcid residuesTranscarbamylasesComplementary DNAAmino acidsMessenger RNARat enzymeNucleotidesCatalytic site
1984
Bacteriophage T4 gene 44 DNA polymerase accessory protein. Sequences of gene 44 and its protein product.
Spicer E, Nossal N, Williams K. Bacteriophage T4 gene 44 DNA polymerase accessory protein. Sequences of gene 44 and its protein product. Journal Of Biological Chemistry 1984, 259: 15425-15432. PMID: 6096371, DOI: 10.1016/s0021-9258(17)42566-x.Peer-Reviewed Original ResearchConceptsGene 44DNA polymerase accessory proteinEscherichia coli RNA polymeraseT4 middle genesT4 DNA replicationAmino acidsPolymerase accessory proteinsPotential regulatory regionsColi RNA polymeraseDirect protein sequencingT4-infected cellsTranslation initiation regionRegA proteinMiddle genesSequence similarityAmino acid compositionDNA replicationRNA polymeraseRegulatory regionsProtein sequencingAccessory proteinsDNA sequencesNucleotide sequenceProtein sequencesNucleotides 5Photochemical 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 studyIrradiationAcidStructure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase
Horwich A, Fenton W, Williams K, Kalousek F, Kraus J, Doolittle R, Konigsberg W, Rosenberg L. Structure and Expression of a Complementary DNA for the Nuclear Coded Precursor of Human Mitochondrial Ornithine Transcarbamylase. Science 1984, 224: 1068-1074. PMID: 6372096, DOI: 10.1126/science.6372096.Peer-Reviewed Original ResearchConceptsComplementary DNALeader peptideOrnithine transcarbamylaseAmino-terminal leader peptideMost mitochondrial proteinsComplete primary structureHuman ornithine transcarbamylaseFree cytoplasmic ribosomesMitochondrial matrix enzymeCultured HeLa cellsMitochondrial proteinsCytoplasmic ribosomesRegulatory elementsNucleotide sequenceStable transformantsMatrix enzymeAsparagine residuesAcidic residuesLarger precursorMature formPrimary structureProtein occursHeLa cellsEscherichia coliAmino acids
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 ResearchConceptsCOOH 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