Literature DB >> 4004773

The assembly of microtubule protein in vitro. The kinetic role in microtubule elongation of oligomeric fragments containing microtubule-associated proteins.

P M Bayley, F M Butler, D C Clark, E J Manser, S R Martin.   

Abstract

The kinetics of assembly were studied for bovine and pig microtubule protein in vitro over a range of conditions of pH, temperature, nucleotide and protein concentration. The kinetics are in general biphasic with two major processes of similar amplitude but separated in rate by one order of magnitude. Rates and amplitudes are complex functions of solution conditions. The rates of the fast phase and the slow phase attain limiting values as a function of increasing protein concentration, and are more stringently limited at pH 6.5 than pH 6.95. Such behaviour indicates that mechanisms other than the condensation polymerization of tubulin dimer become rate-limiting at higher protein concentration. The constancy of the wavelength-dependence of light-scattering and ultrastructural criteria indicate that microtubules of normal morphology are formed in both phases of the assembly process. Electrophoretic analysis of assembling microtubule protein shows that MAP- (microtubule-associated-protein-)rich microtubules are formed during the fast phase. The rate of dissociation of oligomeric species on dilution of microtubule protein closely parallels the fast-phase rate in magnitude and temperature-dependence. We propose that the rate of this process constitutes an upper limit to the rate of the fast phase of assembly. The kinetics of redistribution of MAPs from MAP-rich microtubules may be a factor limiting the slow-phase rate. A working model is derived for the self-assembly of microtubule protein incorporating the dissociation and redistribution mechanisms that impose upper limits to the rates of assembly attainable by bimolecular addition reactions. Key roles are assigned to MAP-containing fragments in both phases of microtubule elongation. Variations in kinetic behaviour with solution conditions are inferred to derive from the nature and properties of fragments formed from oligomeric species after the rapid temperature jump. The model accounts for the limiting rate behaviour and indicates experimental criteria to be applied in evaluating the relative contributions of alternative pathways.

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Year:  1985        PMID: 4004773      PMCID: PMC1144863          DOI: 10.1042/bj2270439

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  48 in total

1.  Purification of tubulin and associated high molecular weight proteins from porcine brain and characterization of microtubule assembly in vitro.

Authors:  G G Borisy; J M Marcum; J B Olmsted; D B Murphy; K A Johnson
Journal:  Ann N Y Acad Sci       Date:  1975-06-30       Impact factor: 5.691

2.  Comparison of the sedimentation properties of microtubule protein oligomers prepared by two different procedures.

Authors:  R B Scheele; G G Borisy
Journal:  Biochem Biophys Res Commun       Date:  1976-05-03       Impact factor: 3.575

3.  Ionic and nucleotide requirements for microtubule polymerization in vitro.

Authors:  J B Olmsted; G G Borisy
Journal:  Biochemistry       Date:  1975-07       Impact factor: 3.162

4.  A kinetic analysis of the assembly of microtubules in vitro.

Authors:  Y Engelborghs; L C De Maeyer; N Overbergh
Journal:  FEBS Lett       Date:  1977-08-01       Impact factor: 4.124

Review 5.  Microtuble assembly: some possible regulatory mechanisms.

Authors:  J B Olmsted; J M Marcum; K A Johnson; C Allen; G G Borisy
Journal:  J Supramol Struct       Date:  1974

6.  Interpretation of the light scattering from long rods.

Authors:  B J Berne
Journal:  J Mol Biol       Date:  1974-11-15       Impact factor: 5.469

7.  Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules.

Authors:  F Gaskin; C R Cantor; M L Shelanski
Journal:  J Mol Biol       Date:  1974-11-15       Impact factor: 5.469

8.  Microtubule assembly in the absence of added nucleotides.

Authors:  M L Shelanski; F Gaskin; C R Cantor
Journal:  Proc Natl Acad Sci U S A       Date:  1973-03       Impact factor: 11.205

9.  The reconstitution of microtubules from purified calf brain tubulin.

Authors:  J C Lee; S N Timasheff
Journal:  Biochemistry       Date:  1975-11-18       Impact factor: 3.162

10.  Assembly and three-dimensional image reconstruction of tubulin hoops.

Authors:  E Mandelkow; R Schultheiss; E M Mandelkow
Journal:  J Mol Biol       Date:  1984-08-15       Impact factor: 5.469

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  7 in total

1.  The effect of solution composition on microtubule dynamic instability.

Authors:  M J Schilstra; P M Bayley; S R Martin
Journal:  Biochem J       Date:  1991-08-01       Impact factor: 3.857

2.  Conformational and assembly properties of nucleotide-depleted tubulin.

Authors:  E J Manser; P M Bayley
Journal:  Biophys J       Date:  1986-01       Impact factor: 4.033

3.  Microtubule assembly kinetics. Changes with solution conditions.

Authors:  J S Barton; D L Vandivort; D H Heacock; J A Coffman; K A Trygg
Journal:  Biochem J       Date:  1987-11-01       Impact factor: 3.857

4.  Dynamic instability of microtubules: Monte Carlo simulation and application to different types of microtubule lattice.

Authors:  S R Martin; M J Schilstra; P M Bayley
Journal:  Biophys J       Date:  1993-08       Impact factor: 4.033

5.  Effects of ATP and cyclic AMP on the in vitro assembly and stability of mammalian brain microtubules.

Authors:  F Pariente; V Prasad; R F Ludueña; R Manso-Martínez
Journal:  Mol Cell Biochem       Date:  1987-03       Impact factor: 3.396

6.  Tubulin-nucleotide interactions. Effects of removal of exchangeable guanine nucleotide on protein conformation and microtubule assembly.

Authors:  E J Manser; P M Bayley
Journal:  Biochem J       Date:  1987-01-01       Impact factor: 3.857

7.  Assembly of chick brain MAP2-tubulin microtubule protein. Characterization of the protein and the MAP2-dependent addition of tubulin dimers.

Authors:  R G Burns
Journal:  Biochem J       Date:  1991-07-01       Impact factor: 3.857

  7 in total

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