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Biophys J. 1999 Dec;77(6):2911-9.

Annealing accounts for the length of actin filaments formed by spontaneous polymerization.

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Department of Chemistry and Biochemistry, University of California-San Diego, La Jolla, California 92093-0365, USA.


We measured the lengths of actin filaments formed by spontaneous polymerization of highly purified actin monomers by fluorescence microscopy after labeling with rhodamine-phalloidin. The length distributions are exponential with a mean of approximately 7 microm (2600 subunits). This length is independent of the initial concentration of actin monomer, an observation inconsistent with a simple nucleation-elongation mechanism. However, with the addition of physically reasonable rates of filament annealing and fragmenting, a nucleation-elongation mechanism can reproduce the observed average length of filaments in two types of experiments: 1) filaments formed from a wide range of highly purified actin monomer concentrations, and 2) filaments formed from 24 microM actin over a range of CapZ concentrations.

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