Engineering cooperativity in biomotor-protein assemblies.

Michael R Diehl; Kechun Zhang; Heun Jin Lee; David A Tirrell

doi:10.1126/science.1122125

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Engineering cooperativity in biomotor-protein assemblies.

Michael R Diehl·Kechun Zhang·Heun Jin Lee·David A Tirrell

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Abstract

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.

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Adenosine Triphosphatases Amino Acid Sequence Elasticity Elastin Hydrolysis Kinesins Microtubules Models, Biological Molecular Motor Proteins Molecular Sequence Data Protein Engineering Protein Structure, Tertiary Proteins Recombinant Proteins Structure-Activity Relationship Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

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Michael R Diehl, Kechun Zhang, Heun Jin Lee, David A Tirrell. 2006-03-10. Engineering cooperativity in biomotor-protein assemblies.. https://doi.org/10.1126/science.1122125

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