Torsional rigidity of single actin filaments and actin-actin bond breaking force under torsion measured directly by in vitro micromanipulation.
Knowledge of the elastic properties of actin filaments is crucial for considering its role in muscle contraction, cellular motile events, and formation of cell shape. The stiffness of actin filaments in the directions of stretching and bending has been determined. In this study, we have directly determined the torsional rigidity and breaking force of single actin filaments by measuring the rotational Brownian motion and tensile strength using optical tweezers and microneedles, respectively. Rotational angular fluctuations of filaments supplied the torsional rigidity as (8.0 +/- 1.2) x 10(-26) Nm2. This value is similar to that deduced from the longitudinal rigidity, assuming the actin filament to be a homogeneous rod. The breaking force of the actin-actin bond was measured while twisting a filament through various angles using microneedles. The breaking force decreased greatly under twist, e.g., from 600-320 pN when filaments were turned through 90 degrees, independent of the rotational direction. Our results indicate that an actin filament exhibits comparable flexibility in the rotational and longitudinal directions, but breaks more easily under torsional load.
Department of Anesthesiology, Osaka University Medical School, Japan.
Y
Y
Tsuda
H
H
Yasutake
A
A
Ishijima
T
T
Yanagida
D000199:Actins / Q000737:chemistry*; D000818:Animals; D008961:Models, Structural; D018482:Muscle, Skeletal; D009218:Myosins / Q000737:chemistry*; D011817:Rabbits; D012399:Rotation; D013314:Stress, Mechanical; D013718:Tensile Strength; D013816:Thermodynamics
D000199:Actins; D009218:Myosins