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
p10 single-stranded nucleic acid binding protein from murine leukemia virus binds metal ions via the peptide sequence Cys26-X2-Cys29-X4-His34-X4-Cys39.
Roberts W, Pan T, Elliott J, Coleman J, Williams K. p10 single-stranded nucleic acid binding protein from murine leukemia virus binds metal ions via the peptide sequence Cys26-X2-Cys29-X4-His34-X4-Cys39. Biochemistry 1989, 28: 10043-7. PMID: 2695161, DOI: 10.1021/bi00452a024.Peer-Reviewed Original ResearchConceptsChemical shiftsMetal ionsSolid-phase synthesis approachCharge transfer bandD absorption bandsMetal binding propertiesChelate complexesUltraviolet absorption spectraCharge transferNMR spectraAbsorption bandsIntense bandAbsorption spectraSynthesis approachBinding propertiesNucleic acidsOligonucleotide bindingIonsComplexesCys residuesSpectraConsiderable interestPpmResiduesBandSite-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 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 Research
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
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 propertiesMetalloproteins