Engineering Cooperativity in Biomotor-Protein Assemblies
Michael R. Diehl,1*
Kechun Zhang,1
Heun Jin Lee,2
David A. Tirrell1
A biosynthetic approach was developed to control and probe cooperativity in multiunit biomotor assemblies by linking molecular motors to artificial protein scaffolds. This approach provides precise control over spatial and elastic coupling between motors. Cooperative interactions between monomeric kinesin-1 motors attached to protein scaffolds enhance hydrolysis activity and microtubule gliding velocity. However, these interactions are not influenced by changes in the elastic properties of the scaffold, distinguishing multimotor transport from that powered by unorganized monomeric motors. These results highlight the role of supramolecular architecture in determining mechanisms of collective transport.
1 Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA.
2 Department of Applied Physics, California Institute of Technology, Pasadena, CA 91125, USA.
* Present address: Department of Bioengineering and Department of Chemistry, Rice University, Houston, TX.
To whom correspondence should be addressed. E-mail: diehl{at}rice.edu
