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Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule.

Abstract：

: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.

journal_name

Elife

journal_title

eLife

authors

Lacey SE,He S,Scheres SH,Carter AP

doi

10.7554/eLife.47145

subject

Has Abstract

pub_date

2019-07-02 00:00:00

issn

2050-084X

pii

47145

journal_volume

8

pub_type

杂志文章

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