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Literature DB >> 10585915

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

D Sept¹, J Xu, T D Pollard, J A McCammon.

Abstract

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.

Entities: Chemical Gene

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Year: 1999 PMID： 10585915 PMCID： PMC1300564 DOI： 10.1016/s0006-3495(99)77124-9

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

34 in total

1. Talin anchors and nucleates actin filaments at lipid membranes. A direct demonstration.

Authors: S Kaufmann; J Käs; W H Goldmann; E Sackmann; G Isenberg
Journal: FEBS Lett Date: 1992-12-14 Impact factor: 4.124

2. Effect of capping protein, CapZ, on the length of actin filaments and mechanical properties of actin filament networks.

Authors: J Xu; J F Casella; T D Pollard
Journal: Cell Motil Cytoskeleton Date: 1999

10. Nucleation-dependent tau filament formation: the importance of dimerization and an estimation of elementary rate constants.

Authors: Erin E Congdon; Sohee Kim; Jonathan Bonchak; Tanakorn Songrug; Anastasios Matzavinos; Jeff Kuret
Journal: J Biol Chem Date: 2008-03-21 Impact factor: 5.157

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

1. Talin anchors and nucleates actin filaments at lipid membranes. A direct demonstration.

2. Effect of capping protein, CapZ, on the length of actin filaments and mechanical properties of actin filament networks.

3. Quantitation of Cap Z in conventional actin preparations and methods for further purification of actin.

4. The mechanical properties of actin gels. Elastic modulus and filament motions.

5. Formation of liquid crystals from actin filaments.

6. Transient kinetic analysis of rhodamine phalloidin binding to actin filaments.

7. The crosslinking of actin and of tropomyosin by glutaraldehyde.

8. Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides.

9. F-actin, a model polymer for semiflexible chains in dilute, semidilute, and liquid crystalline solutions.

10. Yeast actin: polymerization kinetic studies of wild type and a poorly polymerizing mutant.

1. Growth velocities of branched actin networks.

2. A mechanistic model of the actin cycle.

3. Ionic wave propagation along actin filaments.

4. Theory of active transport in filopodia and stereocilia.

Review 5. Use of virtual cell in studies of cellular dynamics.

6. The effects of filament aging and annealing on a model lamellipodium undergoing disassembly by severing.

7. Simulation study of the contribution of oligomer/oligomer binding to capsid assembly kinetics.

8. Stimulation of actin polymerization by filament severing.

9. The effect of branching on the critical concentration and average filament length of actin.

10. Nucleation-dependent tau filament formation: the importance of dimerization and an estimation of elementary rate constants.