Imai, H, Shima, T, Sutoh, K et al. (4 more authors) (2015) Direct observation shows superposition and large scale flexibility within cytoplasmic dynein motors moving along microtubules. Nature Communications, 6. 8179. ISSN 2041-1723
Abstract
Cytoplasmic dynein is a dimeric AAA+ motor protein that performs critical roles in eukaryotic cells by moving along microtubules using ATP. Here using cryo-electron microscopy we directly observe the structure of Dictyostelium discoideum dynein dimers on microtubules at near-physiological ATP concentrations. They display remarkable flexibility at a hinge close to the microtubule binding domain (the stalkhead) producing a wide range of head positions. About half the molecules have the two heads separated from one another, with both leading and trailing motors attached to the microtubule. The other half have the two heads and stalks closely superposed in a front-to-back arrangement of the AAA+ rings, suggesting specific contact between the heads. All stalks point towards the microtubule minus end. Mean stalk angles depend on the separation between their stalkheads, which allows estimation of inter-head tension. These findings provide a structural framework for understanding dynein’s directionality and unusual stepping behaviour.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2015, Author(s). Reproduced in accordance with the publisher's self-archiving policy. This work is licensed under a Creative Commons Attribution 4.0 International License. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) |
Funding Information: | Funder Grant number Human Frontier Science Program RGP0009/2008-C BBSRC BB/K000705/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 18 Sep 2015 12:14 |
Last Modified: | 03 Nov 2017 03:49 |
Published Version: | http://dx.doi.org/10.1038/ncomms9179 |
Status: | Published |
Publisher: | Nature Publishing Group |
Identification Number: | 10.1038/ncomms9179 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:88651 |