Two-stimuli manipulation of a biological motor

Zorica Ristic,Klaus Kemnitz,Alessandro Duci,Werner Zuschratter,Holger Lill,Dirk Bald,Marco Vitali,Christian Goetze

doi:10.1186/1477-3155-7-3

Abstract

F1-ATPase is an enzyme acting as a rotary nano-motor. During catalysis subunits of this enzyme complex rotate relative to other parts of the enzyme. Here we demonstrate that the combination of two input stimuli causes stop of motor rotation. Application of either individual stimulus did not significantly influence motor motion. These findings may contribute to the development of logic gates using single biological motor molecules.

Highlights

We report manipulation of the F1-ATPase motor movement at single molecule level by concerted optical and chemical input stimuli
Biological nano-scale motors fulfil a broad range of tasks in living cells
Kinesin and dynein move in linear fashion

Summary

Introduction

We report manipulation of the F1-ATPase motor movement at single molecule level by concerted optical and chemical input stimuli. We combined an optical stimulus (high-intensity illumination) with a chemical stimulus (rhodamine 6G), on the rotary movement of single F1 molecules. Rotation Assay F1-ATPase was biotinylated at a single cysteine residue in subunit γ using biotin-(PEAC)5-maleimide (Dojindo, Japan), as described elsewhere [10]. Motor movement in absence of input stimuli ATP-driven rotation of F1-ATPase subunit γ was visualized by attachment of a bead to the γ subunit (Fig. 1a) [7,11], typical time courses of the rotational movement of two

Results

Conclusion