Actin and Myosin in pea tendrils
Related Experiment Video
Updated: Aug 8, 2026

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
Published on: May 4, 2022
1Laboratory of Biochemistry, College of Biological Sciences, Beijing Agricultural University, Beijing 100094, People's Republic of China.
Abstract:
We demonstrate here the presence of actin and myosin in pea (Pisum sativum L.) tendrils. The molecular weight of tendril actin is 43,000, the same as rabbit skeletal muscle actin. The native molecular weight of tendril myosin is about 440,000. Tendril myosin is composed of two heavy chains of molecular weight approximately 165,000 and four (two pairs) light chains of 17,000 and 15,000. At high ionic strength, the ATPase activity of pea tendril myosin is activated by K(+)-EDTA and Ca(2+) and is inhibited by Mg(2+). At low ionic strength, the Mg(2+)-ATPase activity of pea tendril myosin is activated by rabbit skeletal muscle F-actin. Superprecipitation occurred after incubation at room temperature when ATP was added to the crude actomyosin extract. It is suggested that the interaction of actin and myosin may play a role in the coiling movement of pea tendril.
Related Concept Videos
Actin and Myosin in Muscle Contraction
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...
The Role of Actin and Myosin in Non-muscle Cells
Formation of Higher-order Actin Filaments
The high-order actin networks...
Introduction to Actin
Actin Treadmilling

