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The structural kinetics of switch-1 and the neck linker explain the functions of kinesin-1 and Eg5.


ABSTRACT: 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.

SUBMITTER: Muretta JM 

PROVIDER: S-EPMC4672802 | biostudies-literature | 2015 Dec

REPOSITORIES: biostudies-literature

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The structural kinetics of switch-1 and the neck linker explain the functions of kinesin-1 and Eg5.

Muretta Joseph M JM   Jun Yonggun Y   Gross Steven P SP   Major Jennifer J   Thomas David D DD   Rosenfeld Steven S SS  

Proceedings of the National Academy of Sciences of the United States of America 20151116 48


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  ...[more]

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