1991
Single‐stranded DNA binding proteins (SSBs) from prokaryotic transmissible plasmids
Ruvolo P, Keating K, Williams K, Chase J. Single‐stranded DNA binding proteins (SSBs) from prokaryotic transmissible plasmids. Proteins Structure Function And Bioinformatics 1991, 9: 120-134. PMID: 2008432, DOI: 10.1002/prot.340090206.Peer-Reviewed Original ResearchConceptsAmino acid residuesSSB proteinDNA bindingE. coli SSB proteinAcid residuesHelix-destabilizing proteinsEscherichia coli SSBAmino acid sequenceNH2-terminal regionCOOH-terminal regionProteins divergeSequence comparisonProtein sequencesSequence homologyAcid sequenceF plasmidPhe-60Trp-40Trp-54NH2-terminalTerminal thirdDNA binding studiesElongation rateTyr-70Protein
1990
Purification and functional characterization of adenovirus ts111A DNA-binding protein. Fluorescence studies of protein-nucleic acid binding.
Meyers M, Keating K, Roberts W, Williams K, Chase J, Horwitz M. Purification and functional characterization of adenovirus ts111A DNA-binding protein. Fluorescence studies of protein-nucleic acid binding. Journal Of Biological Chemistry 1990, 265: 5875-5882. PMID: 2318838, DOI: 10.1016/s0021-9258(19)39444-x.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 ProteinsZinc
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