1991
Analysis of cDNA clones for Acanthamoeba profilin‐I and profilin‐II shows end to end homology with vertebrate profilins and a small family of profilin genes
Pollard T, Rimm D. Analysis of cDNA clones for Acanthamoeba profilin‐I and profilin‐II shows end to end homology with vertebrate profilins and a small family of profilin genes. Cytoskeleton 1991, 20: 169-177. PMID: 1751969, DOI: 10.1002/cm.970200209.Peer-Reviewed Original ResearchConceptsProfilin IIDNA sequencesProtein sequencesAcanthamoeba profilinGenomic DNA fragmentsFull-length cDNAFamily of proteinsProfilin geneAncestral precursorDifferent phylaInvariant residuesAdditional genesCDNA clonesLength cDNAConservative substitutionsPairwise identityDNA fragmentsSouthern blotNorthern blotGenesProfilinAmino acidsSmall familyCDNAConsiderable divergence
1990
Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. I. High resolution epitope mapping and characterization of monoclonal antibody binding sites.
Rimm DL, Kaiser DA, Bhandari D, Maupin P, Kiehart DP, Pollard TD. Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. I. High resolution epitope mapping and characterization of monoclonal antibody binding sites. Journal Of Cell Biology 1990, 111: 2405-2416. PMID: 1703536, PMCID: PMC2116414, DOI: 10.1083/jcb.111.6.2405.Peer-Reviewed Original ResearchIdentification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions.
Sinard JH, Rimm DL, Pollard TD. Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. II. Assembly properties of tails with NH2- and COOH-terminal deletions. Journal Of Cell Biology 1990, 111: 2417-2426. PMID: 2177477, PMCID: PMC2116375, DOI: 10.1083/jcb.111.6.2417.Peer-Reviewed Original ResearchMeSH KeywordsAcanthamoebaAnimalsBase SequenceBinding SitesChromatographyChromatography, DEAE-CelluloseChromatography, GelChromosome DeletionCloning, MolecularDurapatiteElectrophoresis, Polyacrylamide GelEscherichia coliHydroxyapatitesKineticsMacromolecular SubstancesMagnesiumMicroscopy, ElectronMolecular Sequence DataMolecular WeightMyosinsPotassium ChlorideRecombinant Fusion ProteinsScattering, RadiationConceptsFusion proteinMyosin IIMyosin-II tailAntiparallel tetramersAmino acidsAmino acid residuesNative myosin IIRecombinant fusion proteinSequence altersAcid residuesTail sequencesNH2-terminalNonhelical domainAcanthamoeba myosin IIFunctional regionsProteinParacrystal formationAntiparallel dimerAssembly propertiesDimerization mechanismResiduesTerminal deletionDeletionAssemblyTight packing
1989
Purification and characterization of an Acanthamoeba nuclear actin-binding protein.
Rimm DL, Pollard TD. Purification and characterization of an Acanthamoeba nuclear actin-binding protein. Journal Of Cell Biology 1989, 109: 585-591. PMID: 2760108, PMCID: PMC2115709, DOI: 10.1083/jcb.109.2.585.Peer-Reviewed Original ResearchConceptsActin-binding proteinsMyosin ITwo-dimensional peptide mapsAcanthamoeba myosin ICell fractionationATP-insensitive mannerCross-reactive proteinNuclear localizationAffinity-purified antibodiesAbsence of actinMyosin I.Actin filamentsProteinPeptide mapsMonoclonal antibodiesATPase activityPolyclonal antiserumProteolytic productsStokes radiusPolyclonal antibodiesCross-reactive monoclonal antibodiesColumn chromatographyPolypeptideActinDNALocation of the head-tail junction of myosin.
Rimm DL, Sinard JH, Pollard TD. Location of the head-tail junction of myosin. Journal Of Cell Biology 1989, 108: 1783-1789. PMID: 2715178, PMCID: PMC2115540, DOI: 10.1083/jcb.108.5.1783.Peer-Reviewed Original ResearchConceptsMyosin IIHeptad repeatAcanthamoeba myosin IIHead-tail junctionCoiled-coil structureHydrophobic amino acidsNative myosin IIIdentical polypeptidesNH2 terminusMyosin-II tailNonmuscle myosinProteolytic separationLines of evidenceShort tailAmino acidsPosition 847RepeatsMyosinResiduesTailMyosin moleculesHeptadTerminusMonoclonal antibodiesPolypeptideNew plasmid vectors for high level synthesis of eukaryotic fusion proteins in Escherichia coli
Rimm D, Pollard T. New plasmid vectors for high level synthesis of eukaryotic fusion proteins in Escherichia coli. Gene 1989, 75: 323-327. PMID: 2653968, DOI: 10.1016/0378-1119(89)90278-3.Peer-Reviewed Original ResearchConceptsFusion proteinBacterial proteinsPlasmid vectorEscherichia coliCloning sitePlasmid vector systemTotal soluble proteinEukaryotic fusion proteinsSoluble recombinant proteinInsertion of sequencesEukaryotic proteinsMultiple cloning sitePlasmid expression vectorTrpE proteinNew plasmid vectorRecombinant proteinsSoluble proteinExpression vectorTail sequencesAmino acidsProteinVector systemSequenceColiCell suspensions
1988
Resolution of Acanthamoeba castellanii chromosomes by pulsed field gel electrophoresis and construction of the initial linkage map
Rimm D, Pollard T, Hieter P. Resolution of Acanthamoeba castellanii chromosomes by pulsed field gel electrophoresis and construction of the initial linkage map. Chromosoma 1988, 97: 219-223. PMID: 3219918, DOI: 10.1007/bf00292964.Peer-Reviewed Original ResearchMeSH KeywordsAcanthamoebaAnimalsChromosome MappingDNA ProbesElectrophoresis, Agar GelGenetic LinkageKaryotypingConceptsChromosome-sized DNA moleculesMyosin II geneGel electrophoresisDNA moleculesField gel electrophoresisNon-allelic genesProtozoan Acanthamoeba castellaniiDifferent chromosomal bandsLower eukaryotesLinkage mapSmall chromosomesLarge chromosomesLinkage groupsElectrophoretic karyotypeChromosomal bandsChromosome bandsMyosin IBChromosomesAcanthamoeba castellaniiGenesBiochemical researchElectrophoresisEukaryotesDictyosteliumFungi