Direct observation of the rotation of F1-ATPase
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Summary
It is shown that a single molecule of F1-ATPase acts as a rotary motor, the smallest known, by direct observation of its motion by attaching a fluorescent actin filament to the γ-subunit as a marker, which enabled us to observe this motion directly.
- Type
- article
- Published
- 1997-03-20
- Cited by
- 2,135
- References
- 22
- OpenAlex
- https://openalex.org/W2074033410
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:4369582
Keywords
Protein filament, Biophysics, F-ATPase, ATPase, Protein subunit
References
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- Transcription Against an Applied Force
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- Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay.
- Single myosin molecule mechanics: piconewton forces and nanometre steps
- Intersubunit rotation in active F-ATPase
- Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
- The proton flux through the bacterial flagellar motor.
- Rotation of subunits during catalysis by Escherichia coli F1-ATPase.
- Nucleotide-dependent Movement of the ε Subunit between α and β Subunits in the Escherichia coli F1F0-type ATPase*
- ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the gamma subunit relative to the beta subunits.
Cited by
- F(1)-ATPase: a prototypical rotary molecular motor.
- Subunit II (b') and Not Subunit I (b) of Photosynthetic ATP Synthases is Equivalent to Subunit b of the ATP Synthases from Nonphotosynthetic Eubacteria. Evidence for a New Assignment of b-Type F0 Subunits
- The development of new biotechnologies using metalloprotein design.
- Solution Structure of the ε Subunit of the F1-ATPase from Escherichia coli and Interactions of This Subunit with β Subunits in the Complex*
- The petite mutation in yeasts: 50 years on.
- F‐ATPase: specific observation of the rotating c subunit oligomer of EFoEF1
- On what makes the gamma subunit spin during ATP hydrolysis by F(1).
- Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex.
- Bovine Coupling Factor 6, with Just 14.5% Shared Identity, Replaces Subunit h in the Yeast ATP Synthase*
- Powering an inorganic nanodevice with a biomolecular motor.
- 8-N(3)-3'-biotinyl-ATP, a novel monofunctional reagent: differences in the F(1)- and V(1)-ATPases by means of the ATP analogue.
- Real-Time Single-Molecule Imaging of the Infection Pathway of an Adeno-Associated Virus
- Linear and rotary molecular motors.
- A model for the cooperative free energy transduction and kinetics of ATP hydrolysis by F1-ATPase
- New Insight into the Structure and Regulation of the Plant Vacuolar H+-ATPase
- Structure and Properties of the Clathrin-Coated Vesicle and Yeast Vacuolar V-ATPases
- The ion channel of F-ATP synthase is the target of toxic organotin compounds.
- The rotor tip inside a bearing of a thermophilic F1-ATPase is dispensable for torque generation.
- Plant proton pumps
- Neither Helix in the Coiled Coil Region of the Axle of F1-ATPase Plays a Significant Role in Torque Production
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