Rc. Moore et al., ELONGATION FACTOR-1-ALPHA STABILIZES MICROTUBULES IN A CALCIUM CALMODULIN-DEPENDENT MANNER/, Cell motility and the cytoskeleton, 41(2), 1998, pp. 168-180
Elongation factor-1 alpha. (EF-1 alpha), a highly conserved protein na
med for its role in protein translation, is also a microtubule-associa
ted protein (MAP). We used high-resolution differential interference c
ontrast microscopy to quantify the effect of substoichiometric amounts
of EF-1 alpha (isolated from Daucus carota) on the dynamic instabilit
y of microtubules assembled in vitro from either animal or plant tubul
in. EF-1 alpha modulates the dynamic behavior of microtubules assemble
d from either tubulin source, resulting in longer and more persistent
microtubules. EF-1(alpha), at a 1:20 molar ratio to tubulin, significa
ntly (P < 0.05) reduces the frequency of catastrophe threefold and dec
reases shortening velocities almost twofold for microtubules assembled
from animal tubulin. For microtubules assembled from plant tubulin, s
ubstoichiometric amounts of EF-1 alpha significantly (P < 0.05) suppre
ss the frequency of catastrophe greater than twofold and causes an alm
ost threefold reduction in shortening velocities. Elongation velocitie
s increase almost twofold and rescues, which are not observed in the a
bsence of EF-1 alpha, occur. In addition, calcium/calmodulin (Ca2+/CaM
), which regulates the ability of EF-1 alpha to bundle taxol-stabilize
d microtubules in vitro, also modulates the effect of EF-1 alpha on th
e dynamic behavior of microtubules assembled in vitro from animal tubu
lin. Microtubule severing in the presence of EF-1 alpha was never obse
rved. These data support the hypothesis that EF-1 alpha modulates the
dynamic behavior of microtubules assembled in vitro in a Ca2+/CaM-depe
ndent manner. Cell Motil. Cytoskeleton 41:168-180, 1998. (C) 1998 Wile
y-Liss, Inc.