Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 112, Issue 48, Pages E6606-E6613Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1512305112
Keywords
kinesin; transient kinetics; time-resolved fluorescence; molecular motor; fluorescence resonance energy transfer
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Funding
- National Institutes of Health Grants [GM102875, NS073610, AR32961]
- American Heart Association Grant [14SDG20480032]
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Kinesins perform mechanical work to power a variety of cellular functions, from mitosis to organelle transport. Distinct functions shape distinct enzymologies, and this is illustrated by comparing kinesin-1, a highly processive transport motor that can work alone, to Eg5, a minimally processive mitotic motor that works in large ensembles. Although crystallographic models for both motors reveal similar structures for the domains involved in mechanochemical transduction-including switch-1 and the neck linker-how movement of these two domains is coordinated through the ATPase cycle remains unknown. We have addressed this issue by using a novel combination of transient kinetics and time-resolved fluorescence, which we refer to as structural kinetics, to map the timing of structural changes in the switch-1 loop and neck linker. We find that differences between the structural kinetics of Eg5 and kinesin-1 yield insights into how these two motors adapt their enzymologies for their distinct functions.
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