Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 106, Issue 42, Pages 17741-17746Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0905177106
Keywords
kinesin; motor proteins; single-molecule fluorescence; Forster resonance energy transfer
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Funding
- Research Council for Earth and Life Sciences
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek
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The motor protein Kinesin-1 drives intracellular transport along microtubules, with each of its two motor domains taking 16-nm steps in a hand-over-hand fashion. The way in which a single-motor domain moves during a step is unknown. Here, we use Forster resonance energy transfer (FRET) between fluorescent labels on both motor domains of a single kinesin. This approach allows us to resolve the relative distance between the motor domains and their relative orientation, on the submillisecond timescale, during processive stepping. We observe transitions between high and low FRET values for certain kinesin constructs, depending on the location of the labels. These results reveal that, during a step, a kinesin motor domain dwells in a well-defined intermediate position for approximate to 3 ms.
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