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Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule
Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk. We address how cytoplasmic and axonemal dynein MTBDs bind mic...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6629372/ https://www.ncbi.nlm.nih.gov/pubmed/31264960 http://dx.doi.org/10.7554/eLife.47145 |
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author | Lacey, Samuel E He, Shaoda Scheres, Sjors HW Carter, Andrew P |
author_facet | Lacey, Samuel E He, Shaoda Scheres, Sjors HW Carter, Andrew P |
author_sort | Lacey, Samuel E |
collection | PubMed |
description | Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk. We address how cytoplasmic and axonemal dynein MTBDs bind microtubules at near atomic resolution. We decorated microtubules with MTBDs of cytoplasmic dynein-1 and axonemal dynein DNAH7 and determined their cryo-EM structures using helical Relion. The majority of the MTBD is rigid upon binding, with the transition to the high-affinity state controlled by the movement of a single helix at the MTBD interface. DNAH7 contains an 18-residue insertion, found in many axonemal dyneins, that contacts the adjacent protofilament. Unexpectedly, we observe that DNAH7, but not dynein-1, induces large distortions in the microtubule cross-sectional curvature. This raises the possibility that dynein coordination in axonemes is mediated via conformational changes in the microtubule. |
format | Online Article Text |
id | pubmed-6629372 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-66293722019-07-17 Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule Lacey, Samuel E He, Shaoda Scheres, Sjors HW Carter, Andrew P eLife Structural Biology and Molecular Biophysics Dyneins are motor proteins responsible for transport in the cytoplasm and the beating of axonemes in cilia and flagella. They bind and release microtubules via a compact microtubule-binding domain (MTBD) at the end of a coiled-coil stalk. We address how cytoplasmic and axonemal dynein MTBDs bind microtubules at near atomic resolution. We decorated microtubules with MTBDs of cytoplasmic dynein-1 and axonemal dynein DNAH7 and determined their cryo-EM structures using helical Relion. The majority of the MTBD is rigid upon binding, with the transition to the high-affinity state controlled by the movement of a single helix at the MTBD interface. DNAH7 contains an 18-residue insertion, found in many axonemal dyneins, that contacts the adjacent protofilament. Unexpectedly, we observe that DNAH7, but not dynein-1, induces large distortions in the microtubule cross-sectional curvature. This raises the possibility that dynein coordination in axonemes is mediated via conformational changes in the microtubule. eLife Sciences Publications, Ltd 2019-07-02 /pmc/articles/PMC6629372/ /pubmed/31264960 http://dx.doi.org/10.7554/eLife.47145 Text en © 2019, Lacey et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Structural Biology and Molecular Biophysics Lacey, Samuel E He, Shaoda Scheres, Sjors HW Carter, Andrew P Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule |
title | Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule |
title_full | Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule |
title_fullStr | Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule |
title_full_unstemmed | Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule |
title_short | Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule |
title_sort | cryo-em of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule |
topic | Structural Biology and Molecular Biophysics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6629372/ https://www.ncbi.nlm.nih.gov/pubmed/31264960 http://dx.doi.org/10.7554/eLife.47145 |
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