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 Lettjournal_title
FEBS lettersauthors
Krouglova T,Amayed P,Engelborghs Y,Carlier MFdoi
10.1016/s0014-5793(03)00636-7keywords:
subject
Has Abstractpub_date
2003-07-10 00:00:00pages
365-8issue
2-3eissn
0014-5793issn
1873-3468pii
S0014579303006367journal_volume
546pub_type
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