Control of a biomolecular motor-powered nanodevice with an engineered chemical switch.
The biophysical and biochemical properties of motor proteins have been well-studied, but these motors also show promise as mechanical components in hybrid nano-engineered systems. The cytoplasmic F(1) fragment of the adenosine triphosphate synthase (F1-ATPase) can function as an ATP-fuelled rotary motor and has been integrated into self-assembled nanomechanical systems as a mechanical actuator. Here we present the rational design, construction and analysis of a mutant F1-ATPase motor containing a metal-binding site that functions as a zinc-dependent, reversible on/off switch. Repeated cycles of zinc addition and removal by chelation result in inhibition and restoration, respectively, of both ATP hydrolysis and motor rotation of the mutant, but not of the wild-type F1 fragment. These results demonstrate the ability to engineer chemical regulation into a biomolecular motor and represent a critical step towards controlling integrated nanomechanical devices at the single-molecule level.
Liu
Haiqing
H
Department of Bioengineering, University of California, Los Angeles, California 90095, USA.
Schmidt
Jacob J
JJ
Bachand
George D
GD
Rizk
Shahir S
SS
Looger
Loren L
LL
Hellinga
Homme W
HW
Montemagno
Carlo D
CD
D000199:Actins / Q000502:physiology; D000251:Adenosine Triphosphatases / Q000187:drug effects / Q000378:metabolism*; D001407:Bacillus / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D004791:Enzyme Inhibitors / Q000378:metabolism; D004867:Equipment Design; D019544:Equipment Failure Analysis / Q000379:methods; D005246:Feedback; D006706:Homeostasis / Q000502:physiology; D008422:Materials Testing / Q000379:methods; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000138:chemical synthesis* / Q000235:genetics / Q000502:physiology*; D009038:Motion; D009068:Movement / Q000502:physiology*; D016297:Mutagenesis, Site-Directed; D036103:Nanotechnology / Q000295:instrumentation / Q000379:methods*; D012680:Sensitivity and Specificity; D015032:Zinc / Q000378:metabolism* / Q000494:pharmacology
D000199:Actins; D004791:Enzyme Inhibitors; D020409:Molecular Motor Proteins; D000251:Adenosine Triphosphatases; D015032:Zinc