Reversible dissociation of the alpha beta dimer of tubulin from bovine brain
The reversible, concentration-dependent dissociation of the alpha beta dimer of bovine brain tubulin (purified by phosphocellulose chromatography) has been demonstrated by equilibrium ultracentrifugation. The dissociation constant is approximately 8 X 10(-7) M at 4.6 degrees C in PM buffer (0.1 M piperazine-N, N'-bis(2-ethanesulfonic acid), 2 mM ethylene glycol bis (beta-aminoethyl ether)-N, N'-tetraacetic acid, 1 mM MgSO4, 0.1 MM guanosine triphosphate, 2mM dithioerythritol, at pH 6.9). This result was confirmed by observation of an appropriate dependence of the sedimentation coefficient of very dilute (is less than 0.5 mg/mL) tubulin on its concentration. Small zone gel filtration experiments on Bio-Gel P-150 also demonstrated an increase in peak elution volume with decreasing column load concentration. Reversibility of the dissociation was demonstrated directly by sedimentation velocity and gel filtration ion experiments on tubulin reconcentrated from dilute solution by pressure ultrafiltration. Control experiments accompanying the sedimentation equilibrium experiments showed that this tubulin retained, under the conditions of the experiments, both its ability to form microtubules and more than 70% of its initial colchicine-...Continue Reading
In vitro assembly of pure tubulin into microtubules in the absence of microtubule-associated proteins and glycerol
Interaction of chemotactic factors with human macrophages. Induction of transmembrane potential changes
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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
Properties of tubulin in unfertilized sea urchin eggs. Quantitation and characterization by the colchicine-binding reaction
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Tubulin dimer formation via the release of alpha- and beta-tubulin monomers from multimolecular complexes
The irreversibility of subunit associations in glucose-6-phosphate dehydrogenase and a suggestion regarding an early step in cellular morphogenesis
Molar absorptivity and A1%1 cm values for proteins at selected wavelengths of the ultraviolet and visible regions--XVIII
Association states of tubulin in the presence and absence of microtubule-associated proteins. Analysis by electric birefringence
The effect of ruthenium red on the assembly and disassembly of microtubules and on rapid axonal transport
A comparison of weight average and direct boundary fitting of sedimentation velocity data for indefinite polymerizing systems
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Phosphorylation controls the interaction of the connexin43 C-terminal domain with tubulin and microtubules
Cyclic nucleotide phosphodiesterase activity in 10-nm filaments and microtubule preparations from bovine brain
Alpha-tubulin influences nucleotide binding to beta-tubulin: an assay using picomoles of unpurified protein
The C terminus of tubulin, a versatile partner for cationic molecules: binding of Tau, polyamines, and calcium.
Systematic identification of tubulin-interacting fragments of the microtubule-associated protein Tau leads to a highly efficient promoter of microtubule assembly.
The PN2-3 domain of centrosomal P4.1-associated protein implements a novel mechanism for tubulin sequestration
Microtubules and microtubule-associated proteins from the nematode Caenorhabditis elegans: periodic cross-links connect microtubules in vitro
A reevaluation of the structure of purified tubulin in solution: evidence for the prevalence of oligomers over dimers at room temperature
Is microtubule assembly a biphasic process? A fluorimetric study using 4',6-diamidino-2-phenylindole as a probe
Synthesis and evaluation of 2-diazo-3,3,3-trifluopropanoyl derivatives of colchicine and podophyllotoxin as photoaffinity labels: reactivity, photochemistry, and tubulin binding
Polyamine sharing between tubulin dimers favours microtubule nucleation and elongation via facilitated diffusion
Activation of tubulin assembly into microtubules upon a series of repeated femtosecond laser impulses
Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
Fluorescence correlation spectroscopy analysis of the dynamics of tubulin interaction with RB3, a stathmin family protein
Structure of tubulin C-terminal domain obtained by subtilisin treatment. The major alpha and beta tubulin isotypes from pig brain are glutamylated
Evidence for the spontaneous formation of disulfide crosslinked aggregates of tubulin during nondenaturing electrophoresis
Kinetic and thermodynamic aspects of tubulin-ligand interactions: binding of the colchicine analog 2-methoxy-5-(2',3',4'-trimethoxyphenyl) tropone
The interaction between lipid derivatives of colchicine and tubulin: consequences of the interaction of the alkaloid with lipid membranes
Design, synthesis and biological evaluation of a simplified fluorescently labeled discodermolide as a molecular probe to study the binding of discodermolide to tubulin
Correct diffusion coefficients of proteins in fluorescence correlation spectroscopy. Application to tubulin oligomers induced by Mg2+ and Paclitaxel
Separation of tubulin from microtubule-associated proteins on phosphocellulose. Accompanying alterations in concentrations of buffer components
Identification of the major 68,000-dalton protein of microtubule preparations as a 10-nm filament protein and its effects on microtubule assembly in vitro
Conformational states of tubulin liganded to colchicine, tropolone methyl ether, and podophyllotoxin
Purification, characterization, and assembly properties of tubulin from unfertilized eggs of the sea urchin Strongylocentrotus purpuratus
Polymorphism of tubulin oligomers in the presence of microtubule-associated proteins. Implications in microtubule assembly
Microtubule elongation and guanosine 5'-triphosphate hydrolysis. Role of guanine nucleotides in microtubule dynamics
Effect of tubulin binding and self-association on the near-ultraviolet circular dichroic spectra of colchicine and analogues
Thermodynamics of tubulin polymerization into zinc sheets: assembly is not regulated by GTP hydrolysis
Modulation of the stathmin-like microtubule destabilizing activity of RB3, a neuron-specific member of the SCG10 family, by its N-terminal domain.
Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer.
High-speed photothermal off-resonance atomic force microscopy reveals assembly routes of centriolar scaffold protein SAS-6
Direct photoaffinity labeling of cysteine-295 of alpha-tubulin by guanosine 5'-triphosphate bound in the nonexchangeable site.
Dissociation of the tubulin dimer is extremely slow, thermodynamically very unfavorable, and reversible in the absence of an energy source
Macromolecular interaction of halichondrin B analogues eribulin (E7389) and ER-076349 with tubulin by analytical ultracentrifugation
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