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
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
1987
Isolation of cDNA clones coding for human tissue factor: primary structure of the protein and cDNA.
Spicer E, Horton R, Bloem L, Bach R, Williams K, Guha A, Kraus J, Lin T, Nemerson Y, Konigsberg W. Isolation of cDNA clones coding for human tissue factor: primary structure of the protein and cDNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 5148-5152. PMID: 3037536, PMCID: PMC298811, DOI: 10.1073/pnas.84.15.5148.Peer-Reviewed Original ResearchConceptsMature proteinPrimary structureHuman placental cDNA libraryAmino acid sequenceHigh molecular weight precursorTissue factor genePlacental cDNA librarySequence data banksCarbohydrate attachment sitesSingle polypeptide chainMolecular weight precursorDependent serine proteaseSignificant homologyCDNA clonesCDNA librarySequence dataLeader sequenceNucleotide sequenceFactor genesAcid sequenceTissue factorExtracellular domainLambda phageDistinct domainsPolypeptide chain
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 transcriptsProtein 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 ResearchHigh pressure liquid chromatography purification of UP1 and UP2, two related single-stranded nucleic acid-binding proteins from calf thymus.
Merrill B, LoPresti M, Stone K, Williams K. High pressure liquid chromatography purification of UP1 and UP2, two related single-stranded nucleic acid-binding proteins from calf thymus. Journal Of Biological Chemistry 1986, 261: 878-883. PMID: 3941105, DOI: 10.1016/s0021-9258(17)36178-1.Peer-Reviewed Original Research
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 5
1983
F sex factor encodes a single-stranded DNA binding protein (SSB) with extensive sequence homology to Escherichia coli SSB.
Chase J, Merrill B, Williams K. F sex factor encodes a single-stranded DNA binding protein (SSB) with extensive sequence homology to Escherichia coli SSB. Proceedings Of The National Academy Of Sciences Of The United States Of America 1983, 80: 5480-5484. PMID: 6351061, PMCID: PMC384281, DOI: 10.1073/pnas.80.18.5480.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCarrier ProteinsEscherichia coliPlasmidsProtein ConformationTemperatureConceptsF sex factorE. coli SSBAmino acid residuesE. coli SSB proteinAcid residuesEscherichia coli SSBDNA binding proteinE. coli proteinsShine-Dalgarno sequenceAmino acid sequenceExtensive sequence homologyNH2-terminal regionSex factorSSB proteinEvolutionary significanceColi proteinsDNA replicationPresumptive promoterExtensive homologySequence homologyAcid sequenceDyad symmetryFunctional domainsF plasmidTerminator regions