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...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2019-07-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/47145 |
| _version_ | 1811199571458523136 |
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| author | Samuel E Lacey Shaoda He Sjors HW Scheres Andrew P Carter |
| author_facet | Samuel E Lacey Shaoda He Sjors HW Scheres Andrew P Carter |
| author_sort | Samuel E Lacey |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-04-12T01:49:50Z |
| format | Article |
| id | doaj.art-cdcefc48749b4cbab19416039d806876 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T01:49:50Z |
| publishDate | 2019-07-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-cdcefc48749b4cbab19416039d8068762022-12-22T03:52:58ZengeLife Sciences Publications LtdeLife2050-084X2019-07-01810.7554/eLife.47145Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubuleSamuel E Lacey0https://orcid.org/0000-0002-3807-8888Shaoda He1Sjors HW Scheres2https://orcid.org/0000-0002-0462-6540Andrew P Carter3https://orcid.org/0000-0001-7292-5430MRC Laboratory of Molecular Biology, Cambridge, United KingdomMRC Laboratory of Molecular Biology, Cambridge, United KingdomMRC Laboratory of Molecular Biology, Cambridge, United KingdomMRC Laboratory of Molecular Biology, Cambridge, United KingdomDyneins 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.https://elifesciences.org/articles/47145microtubledyneincryoEMRelionaxonemecilia |
| spellingShingle | Samuel E Lacey Shaoda He Sjors HW Scheres Andrew P Carter Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule eLife microtuble dynein cryoEM Relion axoneme cilia |
| 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 | microtuble dynein cryoEM Relion axoneme cilia |
| url | https://elifesciences.org/articles/47145 |
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