Literature DB >> 6822510

Rate for nucleotide release from tubulin.

B P Brylawski, M Caplow.   

Abstract

The lower limit for the first order rate constant for dissociation of GDP from the tubulin E-site has been determined to be 0.14 s-1; this corresponds to a reaction with a half-life of 5 s. Using this rate constant and the previously determined equilibrium constant for GDP dissociation, equal to 6.1 X 10(-8) M (Zeeberg, B., and Caplow, M. (1979) Biochemistry 18, 3880-3886), the calculated association rate constant is 2.2 X 10(6) M-1 s-1. The tubulin E-site is highly reactive and it is calculated that: the half-life is 5 s for quantitative displacement of E-site bound radioactive GDP, by added excess nonradioactive GDP; the half-life is about 260 ms for isotopic equilibration when a trace amount of radioactive GDP is added to 20 microM tubulin-GDP; the half-life is about 850 ms for re-establishing the equilibrium for GDP binding, when 20 microM tubulin is diluted 20-fold. Thus, tubulin-GDP nucleotide exchange is rapid, so that added radioactive guanine nucleotides can be used in studies of relatively rapid reactions involving the tubulin subunit.

Entities:  

Mesh:

Substances:

Year:  1983        PMID: 6822510

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  9 in total

1.  Op18/stathmin mediates multiple region-specific tubulin and microtubule-regulating activities.

Authors:  N Larsson; B Segerman; B Howell; K Fridell; L Cassimeris; M Gullberg
Journal:  J Cell Biol       Date:  1999-09-20       Impact factor: 10.539

2.  Dissociation of the tubulin dimer is extremely slow, thermodynamically very unfavorable, and reversible in the absence of an energy source.

Authors:  Michael Caplow; Lanette Fee
Journal:  Mol Biol Cell       Date:  2002-06       Impact factor: 4.138

Review 3.  Compare and contrast actin filaments and microtubules.

Authors:  T J Mitchison
Journal:  Mol Biol Cell       Date:  1992-12       Impact factor: 4.138

4.  Interference of GTP hydrolysis in the mechanism of microtubule assembly: an experimental study.

Authors:  M F Carlier; T L Hill; Y Chen
Journal:  Proc Natl Acad Sci U S A       Date:  1984-02       Impact factor: 11.205

5.  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

6.  Oscillations in microtubule polymerization: the rate of GTP regeneration on tubulin controls the period.

Authors:  R Melki; M F Carlier; D Pantaloni
Journal:  EMBO J       Date:  1988-09       Impact factor: 11.598

7.  Effects of random hydrolysis on biofilament length distributions in a shared subunit pool.

Authors:  Sankeert Satheesan; Binayak Banerjee; Dipjyoti Das
Journal:  Biophys J       Date:  2021-12-23       Impact factor: 4.033

8.  Quantifying the Monomer-Dimer Equilibrium of Tubulin with Mass Photometry.

Authors:  Adam Fineberg; Thomas Surrey; Philipp Kukura
Journal:  J Mol Biol       Date:  2020-10-15       Impact factor: 5.469

9.  The free energy for hydrolysis of a microtubule-bound nucleotide triphosphate is near zero: all of the free energy for hydrolysis is stored in the microtubule lattice.

Authors:  M Caplow; R L Ruhlen; J Shanks
Journal:  J Cell Biol       Date:  1994-11       Impact factor: 10.539

  9 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.