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J Biol Chem, Vol. 274, Issue 10, 6234-6243, March 5, 1999

Filament Assembly from Profilin-Actin

Irina Gutsche-Perelroizen, Jean LepaultDagger , Albrecht Ott§, and Marie-France Carlier

From the Laboratoire d'Enzymologie et Biochimie Structurales, Dagger  Centre de Génétique Moléculaire, CNRS, 91198 Gif-sur-Yvette, France and § Institut Curie, Physics Section, 11 rue Pierre et Marie Curie, 75005 Paris, France

Profilin plays a major role in the assembly of actin filament at the barbed ends. The thermodynamic and kinetic parameters for barbed end assembly from profilin-actin have been measured turbidimetrically. Filament growth from profilin-actin requires MgATP to be bound to actin. No assembly is observed from profilin-CaATP-actin. The rate constant for association of profilin-actin to barbed ends is 30% lower than that of actin, and the critical concentration for F-actin assembly from profilin-actin units is 0.3 µM under physiological ionic conditions. Barbed ends grow from profilin-actin with an ADP-Pi cap. Profilin does not cap the barbed ends and is not detectably incorporated into filaments. The EDC-cross-linked profilin-actin complex (PAcov) both copolymerizes with F-actin and undergoes spontaneous self-assembly, following a nucleation-growth process characterized by a critical concentration of 0.2 µM under physiological conditions. The PAcov polymer is a helical filament that displays the same diffraction pattern as F-actin, with layer lines at 6 and 36 nm. The PAcov filaments bound phalloidin with the same kinetics as F-actin, bound myosin subfragment-1, and supported actin-activated ATPase of myosin subfragment-1, but they did not translocate in vitro along myosin-coated glass surfaces. These results are discussed in light of the current models of actin structure.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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