1991
A retrovirus-like zinc domain is essential for translational repression of bacteriophage T4 gene 32
Shamoo Y, Webster K, Williams K, Konigsberg W. A retrovirus-like zinc domain is essential for translational repression of bacteriophage T4 gene 32. Journal Of Biological Chemistry 1991, 266: 7967-7970. PMID: 2022625, DOI: 10.1016/s0021-9258(18)92923-6.Peer-Reviewed Original ResearchConceptsZinc-binding subdomainsGene 32 mRNALevel of translationCooperative bindingBacteriophage T4 gene 32Zinc-binding motifDNA-binding proteinsGene 32 proteinRibosome binding siteT4 gene 32Stem-loop structureTranslational repressionVariety of retrovirusesGene 32Pseudoknot sequencesPlant virusesZinc domainUnstructured regionsBacteriophage T4Sequence homologyAutoregulatory regionGp32RNA pseudoknotsEssential roleProtein
1990
A novel function for zinc(II) in a nucleic acid-binding protein. Contribution of zinc(II) toward the cooperativity of bacteriophage T4 gene 32 protein binding.
Nadler S, Roberts W, Shamoo Y, Williams K. A novel function for zinc(II) in a nucleic acid-binding protein. Contribution of zinc(II) toward the cooperativity of bacteriophage T4 gene 32 protein binding. Journal Of Biological Chemistry 1990, 265: 10389-10394. PMID: 2113053, DOI: 10.1016/s0021-9258(18)86958-7.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-Binding ProteinsDNA, Single-StrandedDNA, ViralElectrophoresis, Polyacrylamide GelEscherichia coliGene Expression RegulationGenes, ViralMutationNucleic Acid DenaturationPoly dA-dTPoly TProtein DenaturationT-PhagesTemperatureThermodynamicsTrypsinTyrosineViral ProteinsZincThe 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
1988
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
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 peptideChromatographyComplexes
1987
The function of zinc in gene 32 protein from T4.
Giedroc D, Keating K, Williams K, Coleman J. The function of zinc in gene 32 protein from T4. Biochemistry 1987, 26: 5251-9. PMID: 3314985, DOI: 10.1021/bi00391a007.Peer-Reviewed Original Research
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 ResearchConceptsGene 32 proteinApo-g32PT4-infected Escherichia coliBacteriophage T4-infected Escherichia coliTyrosine-rich sequenceP-hydroxymercuriphenylsulfonatePlasmid pKC30Sequence CysBacteriophage T4Limited proteolysisConformational elementsEscherichia coliProteinDNAEDTA resultsG32PCysteineFragment ASide chainsPKC30ComplexesProteolysisColiSequenceLinear incorporationZinc metalloproteins involved in replication and transcription
Giedroc D, Keating K, Martin C, Williams K, Coleman J. Zinc metalloproteins involved in replication and transcription. Journal Of Inorganic Biochemistry 1986, 28: 155-169. PMID: 3543219, DOI: 10.1016/0162-0134(86)80079-4.Peer-Reviewed Original ResearchConceptsRNA polymeraseP-hydroxymercuriphenylsulfonateMultisubunit RNA polymerasesGene 32 proteinTranscription initiationDNA binding propertiesTranslational controlProtein essentialDNA replicationAccessory proteinsBacteriophage T7Allosteric roleRPaseBacteriophage T4Apo-g32PZinc metalloproteinsDNA polymeraseElongation ratePolymeraseE. coliProteinBiosynthesisLife cycleBinding propertiesMetalloproteinsSingle-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
Cloning, 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 plasmidSequenceFragmentsCloningRegATranslation
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 studyIrradiationAcid1H NMR (500 MHz) of gene 32 protein--oligonucleotide complexes.
Prigodich R, Casas-Finet J, Williams K, Konigsberg W, Coleman J. 1H NMR (500 MHz) of gene 32 protein--oligonucleotide complexes. Biochemistry 1984, 23: 522-9. PMID: 6367821, DOI: 10.1021/bi00298a019.Peer-Reviewed Original ResearchConceptsN-terminal B-domainGene 32 proteinC-terminal domainCore proteinComplex formationGene 32Bacteriophage T4Bacteriophage fdC-terminalOligonucleotide bindingChemical shift changesTyr residuesB domainAromatic residuesNucleotide basesProteinResiduesLong rotational correlation timeOligonucleotide complexesHigh affinityComplexesShift changesDomainProton resonancesRotational correlation time
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
1982
Crystallization of a tryptic core of the single-stranded DNA binding protein of bacteriophage T4
McKay D, Williams K. Crystallization of a tryptic core of the single-stranded DNA binding protein of bacteriophage T4. Journal Of Molecular Biology 1982, 160: 659-661. PMID: 7175942, DOI: 10.1016/0022-2836(82)90321-7.Peer-Reviewed Original ResearchBacteriophage T4 gene 45. Sequences of the structural gene and its protein product.
Spicer E, Noble J, Nossal N, Konigsberg W, Williams K. Bacteriophage T4 gene 45. Sequences of the structural gene and its protein product. Journal Of Biological Chemistry 1982, 257: 8972-8979. PMID: 6284751, DOI: 10.1016/s0021-9258(18)34228-5.Peer-Reviewed Original ResearchConceptsGene 45T4 late gene transcriptionT4 DNA replication complexRNA polymerase recognitionT4 DNA replicationLate gene transcriptionDNA replication complexTranslation initiation regionNucleotide sequence analysisGenes 46Protein chemistry studiesRegA proteinStructural geneSequence similarityDNA replicationPutative promoterRNA polymeraseReplication complexGene transcriptionProtein productsSequence analysisPrimary structureInitiation regionRIIB genePolymerase recognition
1981
Primary structure of the bacteriophage T4 DNA helix-destabilizing protein.
Williams K, LoPresti M, Setoguchi M. Primary structure of the bacteriophage T4 DNA helix-destabilizing protein. Journal Of Biological Chemistry 1981, 256: 1754-1762. PMID: 6257686, DOI: 10.1016/s0021-9258(19)69872-8.Peer-Reviewed Original ResearchConceptsGene 32 proteinT4 DNA replication proteinsPrimary structureDNA replication proteinsDNA-binding proteinsHelix-destabilizing proteinLimited trypsin digestionGene 32Replication proteinsUnusual stretchesSerine residuesCyanogen bromide cleavageBacteriophage T4DNA bindingSequencing of peptidesAlpha-helixTyrosine residuesBeta sheetNative proteinStaphylococcal proteaseCooperative bindingAmino acidsTryptic peptidesPosition 72ProteinDNA 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