期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 106, 期 42, 页码 17741-17746出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0905177106
关键词
kinesin; motor proteins; single-molecule fluorescence; Forster resonance energy transfer
资金
- Research Council for Earth and Life Sciences
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek
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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