Binding of tropomyosin-troponin to actin increases filament bending stiffness
1Departments of Pathology and Surgery, Children's Hospital, Boston, Massachusetts, 02115, USA.
Abstract:
Rheologic measurements show that the association of tropomyosin-troponin with actin filaments is responsible for the reduction of the internal chain dynamic and increase in the mechanical rigidity of actin filaments. Basing calculations on the linear relation between the plateau modulus, G(N)('), and bending modulus, kappa, I find that tropomyosin-troponin at r(AT) = 7 increases actin filament stiffness by approximately 50%. This is confirmed by dynamic light scattering. Further increases are observed at rising F-actin and constant tropomyosin-troponin concentrations. Tropomyosin-troponin also delays actin assembly and subsequent network formation and increases filament stiffness over time.
Related Concept Videos
Actin and Myosin in Muscle Contraction
The Sarcomere
Each myosin...
Actin Filament Depolymerization
In F-actin, the ADF/cofilin proteins...
Actin Polymerization
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight actin...
Generation of Straight or Branched Actin Filaments
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Formation of Higher-order Actin Filaments
The high-order actin networks...


