1990
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.
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 packingAcanthamoeba myosin-II minifilaments assemble on a millisecond time scale with rate constants greater than those expected for a diffusion limited reaction.
Sinard JH, Pollard TD. Acanthamoeba myosin-II minifilaments assemble on a millisecond time scale with rate constants greater than those expected for a diffusion limited reaction. Journal Of Biological Chemistry 1990, 265: 3654-3660. PMID: 2303471, DOI: 10.1016/s0021-9258(19)39643-7.Peer-Reviewed Original Research
1989
The effect of heavy chain phosphorylation and solution conditions on the assembly of Acanthamoeba myosin-II.
Sinard JH, Pollard TD. The effect of heavy chain phosphorylation and solution conditions on the assembly of Acanthamoeba myosin-II. Journal Of Cell Biology 1989, 109: 1529-1535. PMID: 2793932, PMCID: PMC2115825, DOI: 10.1083/jcb.109.4.1529.Peer-Reviewed Original ResearchConceptsLateral aggregationLow ionic strengthSolution conditionsCritical concentrationIonic strengthLight scatteringMillimolar concentrationsAssembly propertiesAcidic pHExtent of assemblyMoleculesLower tendencyAssemblyMyosin II minifilamentsIonic conditionsPolymerizationMonomersMgCl2AggregationConcentrationMinifilamentsHigh concentrationsFurther modulationPolymerizesThe mechanism of assembly of Acanthamoeba myosin-II minifilaments: minifilaments assemble by three successive dimerization steps.
Sinard JH, Stafford WF, Pollard TD. The mechanism of assembly of Acanthamoeba myosin-II minifilaments: minifilaments assemble by three successive dimerization steps. Journal Of Cell Biology 1989, 109: 1537-1547. PMID: 2793933, PMCID: PMC2115822, DOI: 10.1083/jcb.109.4.1537.Peer-Reviewed Original Research