Fluorescence correlation spectroscopy analysis of the dynamics of tubulin interaction with RB3, a stathmin family protein.

Abstract:

:We have used fluorescence correlation spectroscopy to analyze the interaction of GTP-tubulin with rhodamine-labeled RB3, a neural protein of the stathmin family, and to determine the kinetic pathway of the association process. RB3 displayed slow association-dissociation kinetics with tubulin depending on the square of the tubulin concentration. The values of the apparent association and dissociation rate constants of the complex of two tubulin dimers and RB3 are determined to be (3.52+/-0.14)x10(-3) micro;M(-2)/s and (1.9+/-0.6)x10(-3) s(-1) respectively. The value of the equilibrium dissociation constant for the first tubulin-RB3 interaction is estimated to be >or=7 microM at 20 degrees C.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Krouglova T,Amayed P,Engelborghs Y,Carlier MF

doi

10.1016/s0014-5793(03)00636-7

keywords:

subject

Has Abstract

pub_date

2003-07-10 00:00:00

pages

365-8

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014579303006367

journal_volume

546

pub_type

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