Open AccessApparently irreversible GTP hydrolysis attends tubulin self‐assembly
Author(s) -
ANGELASTRO James M.,
PURICH Daniel L.
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb19150.x
Subject(s) - gtp' , cleavage (geology) , tubulin , hydrolysis , microtubule , polymerization , chemistry , biophysics , depolymerization , bond cleavage , stereochemistry , biochemistry , polymer chemistry , polymer , organic chemistry , enzyme , microbiology and biotechnology , biology , catalysis , paleontology , fracture (geology)
The pathway of GTP hydrolysis associated with microtubule polymerization was investigated using an assay of intermediate 18 O‐exchange reactions. Under a variety of conditions influencing tubulin self‐assembly, GTP was hydrolyzed without any evidence of multiple reversals characteristic of reversible phosphoanhydride‐bond cleavage. These results also accord with published findings that ATP hydrolysis during actin polymerization fails to display intermediate exchange reactions [Carlier, M. F., Pantaloni, D., Evans, J. A., Lambooy, P. K., Korn, E. D. and Webb, M. R. (1988) FEBS Lett. 235, 211–214].