Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding
| Autor: | Anthony J. Roberts, Reiko Ohkura, Peter J. Knight, Kazuo Sutoh, I R Gibbons, Kenji Imamula, Stan A. Burgess, Takahide Kon |
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| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular Dynein Molecular Sequence Data Protozoan Proteins Biology Protein degradation Microtubules Article Protein Structure Secondary 03 medical and health sciences 0302 clinical medicine Structural Biology Microtubule Molecular motor Animals Dictyostelium Amino Acid Sequence Cytoskeleton Molecular Biology 030304 developmental biology Coiled coil Adenosine Triphosphatases 0303 health sciences Binding Sites Dyneins Cell biology Helix Protein folding 030217 neurology & neurosurgery Locomotion Protein Binding |
| Zdroj: | Nature structural & molecular biology |
| ISSN: | 1545-9985 1545-9993 |
| Popis: | Coupling between ATPase and track-binding sites is essential for molecular motors to move along cytoskeletal tracks. In dynein, these sites are separated by a long coiled-coil stalk which must mediate communication between them, yet the underlying mechanism remains unclear. Here we show that changes in registration between the two helices of the coiled coil can perform this function. We locked the coiled coil at three specific registrations using oxidation to disulfides of paired cysteine residues introduced into the two helices. These trapped ATPase activity either in a microtubule-independent high or low state, and microtubule-binding activity either in an ATP-insensitive strong or weak state, depending on the registry of the coiled coil. Our results provide direct evidence that dynein uses sliding between the two helices of the stalk to couple ATPase and microtubule-binding activities during its mechanochemical cycle. |
| Databáze: | OpenAIRE |
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