1999
Identification of the RNA Binding Domain of T4 RegA Protein by Structure-based Mutagenesis*
Gordon J, Sengupta T, Phillips C, O'Malley S, Williams K, Spicer E. Identification of the RNA Binding Domain of T4 RegA Protein by Structure-based Mutagenesis*. Journal Of Biological Chemistry 1999, 274: 32265-32273. PMID: 10542265, DOI: 10.1074/jbc.274.45.32265.Peer-Reviewed Original ResearchConceptsRegA proteinBeta-sheet residuesGel mobility shift assaysRNA gel mobility shift assaysProtein-RNA interactionsMutagenesis of residuesRNA Binding DomainRNA binding siteMobility shift assaysRNA recognition propertiesBeta-sheet regionUnique structural motifMutant proteinsRNA bindingProtein foldsShift assaysBinding domainsMutagenesis studiesStructural domainsDomain IIMutagenesisEquilibrium binding assaysProteinRNABinding sites
1995
Mutagenesis 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
1994
Both RNA-binding domains in heterogenous nuclear ribonucleoprotein A1 contribute toward single-stranded-RNA binding.
Shamoo Y, Abdul-Manan N, Patten A, Crawford J, Pellegrini M, Williams K. Both RNA-binding domains in heterogenous nuclear ribonucleoprotein A1 contribute toward single-stranded-RNA binding. Biochemistry 1994, 33: 8272-81. PMID: 7518244, DOI: 10.1021/bi00193a014.Peer-Reviewed Original ResearchAmino Acid SequenceBinding SitesCircular DichroismCloning, MolecularDNAElectrochemistryHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsHydrogen-Ion ConcentrationMolecular Sequence DataOligonucleotidesPeptide FragmentsPoly UProtein Structure, SecondaryRibonucleoproteinsRNASodium ChlorideThermodynamics
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
1991
Interactions of the A1 heterogeneous nuclear ribonucleoprotein and its proteolytic derivative, UP1, with RNA and DNA: evidence for multiple RNA binding domains and salt-dependent binding mode transitions.
Nadler S, Merrill B, Roberts W, Keating K, Lisbin M, Barnett S, Wilson S, Williams K. Interactions of the A1 heterogeneous nuclear ribonucleoprotein and its proteolytic derivative, UP1, with RNA and DNA: evidence for multiple RNA binding domains and salt-dependent binding mode transitions. Biochemistry 1991, 30: 2968-76. PMID: 1848781, DOI: 10.1021/bi00225a034.Peer-Reviewed Original ResearchAmino Acid SequenceCircular DichroismDNA HelicasesDNA-Binding ProteinsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsKineticsMolecular Sequence DataNucleic Acid DenaturationPoly A-UPoly dA-dTPolydeoxyribonucleotidesPolyribonucleotidesRibonucleoproteinsSpectrometry, FluorescenceThermodynamicsThymus Hormones
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
Synthesis 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 ResearchConceptsBeta 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
Purification 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