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          Institute: MPI für molekulare Zellbiologie und Genetik     Collection: MPI-CBG Publications 2016 (archival)     Display Documents

ID: 732500.0, MPI für molekulare Zellbiologie und Genetik / MPI-CBG Publications 2016 (archival)
Working stroke of the kinesin-14, ncd, comprises two substeps of different direction.
Authors:Nitzsche, Bert; Dudek, Elzbieta; Hajdo, Lukasz; Kasprzak, Andrzej A; Vilfan, Andrej; Diez, Stefan
Date of Publication (YYYY-MM-DD):2016
Title of Journal:Proceedings of the National Academy of Sciences of the United States of America
Issue / Number:43
Sequence Number of Article:E6582-E6589
Copyright:not available
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:Single-molecule experiments have been used with great success to explore the mechanochemical cycles of processive motor proteins such as kinesin-1, but it has proven difficult to apply these approaches to nonprocessive motors. Therefore, the mechanochemical cycle of kinesin-14 (ncd) is still under debate. Here, we use the readout from the collective activity of multiple motors to derive information about the mechanochemical cycle of individual ncd motors. In gliding motility assays we performed 3D imaging based on fluorescence interference contrast microscopy combined with nanometer tracking to simultaneously study the translation and rotation of microtubules. Microtubules gliding on ncd-coated surfaces rotated around their longitudinal axes in an [ATP]- and [ADP]-dependent manner. Combined with a simple mechanical model, these observations suggest that the working stroke of ncd consists of an initial small movement of its stalk in a lateral direction when ADP is released and a second, main component of the working stroke, in a longitudinal direction upon ATP binding.
External Publication Status:published
Document Type:Article
Communicated by:Thüm
Affiliations:MPI für molekulare Zellbiologie und Genetik
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