Working stroke of the kinesin-14, ncd, comprises two substeps of different direction
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- Bert Nitzsche
- Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany;
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- Elzbieta Dudek
- Nencki Institute of Experimental Biology, 02-093 Warsaw, Poland;
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- Lukasz Hajdo
- Nencki Institute of Experimental Biology, 02-093 Warsaw, Poland;
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- Andrzej A. Kasprzak
- Nencki Institute of Experimental Biology, 02-093 Warsaw, Poland;
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- Andrej Vilfan
- J. Stefan Institute, 1000 Ljubljana, Slovenia
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- Stefan Diez
- Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany;
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説明
<jats:title>Significance</jats:title> <jats:p>Kinesin, dynein, and myosin motor proteins are best known for their production of linear force along the axes of cytoskeletal filaments. However, many of these motors can also generate torque manifesting itself by filament rotations around their longitudinal axes when gliding on motor-coated surfaces. By combining the measured longitudinal and angular velocities of microtubules gliding on nonprocessive kinesin-14 motors with a theoretical model we here show that the working stroke of this motor comprises at least two distinct conformational changes. Our observations clarify the temporal order of events in the hydrolysis cycle of kinesin-14, which has not been conclusive from previous structural and single-molecule data. Moreover, our results demonstrate how conformational changes in individual enzymes can be deduced from their ensemble properties.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 113 (43), 6582-, 2016-10-11
Proceedings of the National Academy of Sciences
