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
1986
Gene 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 propertiesMetalloproteins1H NMR (500 MHz) identification of aromatic residues of gene 32 protein involved in DNA binding by use of protein containing perdeuterated aromatic residues and by site-directed mutagenesis.
Prigodich R, Shamoo Y, Williams K, Chase J, Konigsberg W, Coleman J. 1H NMR (500 MHz) identification of aromatic residues of gene 32 protein involved in DNA binding by use of protein containing perdeuterated aromatic residues and by site-directed mutagenesis. Biochemistry 1986, 25: 3666-72. PMID: 3013293, DOI: 10.1021/bi00360a029.Peer-Reviewed Original ResearchConceptsGene 32 proteinTyr-115Aromatic residuesPhe residueDNA binding surfaceAmino acid sequenceSite-directed mutationsSite-directed mutagenesisComplex formationAcid sequenceBinding surfaceUse of proteinsTyr residuesNMR difference spectraTyr-73ProteinResiduesPhenylalanyl residuesDNANMR identificationTyrMutagenesisMutationsTyrosylDifference spectra
1984
1H 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 Research
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 72Protein
1980
Amino acid sequence of the T4 DNA helix-destabilizing protein.
Williams K, LoPresti M, Setoguchi M, Konigsberg W. Amino acid sequence of the T4 DNA helix-destabilizing protein. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 4614-4617. PMID: 6254033, PMCID: PMC349895, DOI: 10.1073/pnas.77.8.4614.Peer-Reviewed Original ResearchConceptsT4 DNA replication proteinsDNA replication proteinsDNA-binding proteinsHelix-destabilizing proteinGene 32 proteinProtein-protein interactionsAmino acid sequenceLimited trypsin digestionProtein self-associationGene 32Replication proteinsUnusual stretchesSerine residuesCyanogen bromide cleavageDNA bindingAcid sequenceTyrosine residuesPrimary structureStaphylococcal proteasePartial proteolysisIntact proteinPosition 73Amino acidsTryptic peptidesProtein
1978
Structural changes in the T4 gene 32 protein induced by DNA polynucleotides.
Williams K, Konigsberg W. Structural changes in the T4 gene 32 protein induced by DNA polynucleotides. Journal Of Biological Chemistry 1978, 253: 2463-2470. PMID: 632279, DOI: 10.1016/s0021-9258(17)38096-1.Peer-Reviewed Original ResearchConceptsGene 32 proteinT4 gene 32 proteinDNA-binding proteinsT4 DNA metabolismTryptic hydrolysisPartial trypsin digestionDNA metabolismGene 32Protein interactionsBacteriophage T4COOH terminusNH2 terminusLimited tryptic hydrolysisCooperative bindingDNA complexesDNA interactionAmino acidsProteinTrypsin digestionDNA polynucleotidesConformational probeTerminusDalton fragmentFragmentsHydrolysis