Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends
1996
Murray, J.W. | Edmonds, B.T. | Liu, G. | Condeelis, J.
Elongation factor 1 alpha (EF1alpha) is an abundant protein that binds aminoacyl-tRNA and ribosomes in a GTP-dependent manner. EF1alpha also interacts with the cytoskeleton by binding and bundling actin filaments and microtubules. In this report, the effect of purified EF1alpha on actin polymerization and depolymerization is examined. At molar ratios present in the cytosol, EF1alpha significantly blocks both polymerization and depolymerization of actin filaments and increases the final extent of actin polymer, while at high molar ratios to actin, EF1alpha nucleates actin polymerization. Although EF1alpha binds actin monomer, this monomer-binding activity does not explain the effects of EF1alpha on actin polymerization at physiological molar ratios. The mechanism for the inhibition of polymerization is related to the actin-bundling activity of EF1alpha. Both ends of the actin filament are inhibited for polymerization and both bundling and the inhibition of actin polymerization are affected by pH within the same physiological range; at high pH both bundling and the inhibition of actin polymerization are reduced. Additionally, it is seen that the binding of aminoacyl-tRNA to EF1alpha releases EF1alpha's inhibiting effect on actin polymerization. These data demonstrate that EF1alpha can alter the assembly of F-actin, a filamentous scaffold on which nonmembrane-associated protein translation may be occurring in vivo.
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