Related Experiment Video
Updated: Jul 29, 2026

Biophysical Characterization of Flagellar Motor Functions
Published on: January 18, 2017
Interaction of bacterial flagellum filaments with skeletal muscle myosin
N A Novikova1, D I Levitsky, A L Metlina
1AN Belozersky Institute of Physico-Chemical Biology, MV Lomonosov Moscow State University, Russia.
Abstract:
Interaction of isolated bacterial flagellum filaments (BFF) and intact flagella from E. coli MS 1350 and B. brevis G.-B.p+ with rabbit skeletal myosin was studied. BFF were shown to coprecipitate with myosin (but not with isolated myosin rod) at low ionic strength, that is, under conditions of myosin aggregation. The data of electron microscopy indicate that filaments of intact bacterial flagella interact with isolated myosin heads (myosin subfragment 1, S1), and this interaction is fully prevented by addition of Mg2+ -ATP. Addition of BFF inhibited both K+ -EDTA- and Ca2+ -ATPase activity of skeletal muscle myosin, but had no effect on its Mg2+ -ATPase activity. Monomeric flagellin did not coprecipitate with myosin and had no effect on its ATPase activities. BFF were shown to compete with F-actin in myosin binding. It is concluded that BFF interact with myosin heads and affect their ATPase activity. Thus, BFF composed of a single protein flagellin are in many respects similar to actin filaments. Common origin of actin and flagellin may be a reason for this similarity.
Related Concept Videos
Overview of Myosin Structure and Function
Actin and Myosin in Muscle Contraction
The Role of Actin and Myosin in Non-muscle Cells
Muscle Contraction
Excitation-Contraction Coupling in Skeletal Muscles
When an action potential...
Flagella and Motility in Bacteria

