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J Biol Chem, Vol. 274, Issue 30, 20970-20976, July 23, 1999
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From the The effect of Arabidopsis
thaliana ADF1 and human ADF on the number of filaments in
F-actin solutions has been examined using a seeded polymerization
assay. ADF did not sever filaments in a catalytic fashion, but
decreased the steady-state length distribution of actin filaments in
correlation with its effect on actin dynamics. The increase in filament
number was modest as compared with the large increase in filament
turnover. ADF did not decrease the length of filaments shorter than 1 µm. ADF promoted the rapid turnover of gelsolin-capped filaments in a
manner dependent on the number of pointed ends. To explain these
results, we propose that, as a consequence of the cooperative binding
of ADF to F-actin, two populations of energetically different filaments
coexist in solution pending a flux of subunits from one to the other.
The ADF-decorated filaments depolymerize rapidly from their pointed ends, while undecorated filaments polymerize. ADF also promotes rapid
turnover of gelsolin-capped filaments in the presence of the pointed
end capper Arp2/3 complex. It is shown that the Arp2/3 complex steadily
generates new barbed ends in solutions of gelsolin-capped filaments,
which represents an important aspect of its function in actin-based motility.
Dynamique du Cytosquelette, Laboratoire
díEnzymologie et Biochimie Structurales, CNRS, 91198 Gif-sur-Yvette, France and the § Unité de
Pathogénicité Microbienne Moléculaire, Institut
Pasteur, Paris, France
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