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.
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
