- EMDB-20821: The Nexin-dynein Regulatory Complex (N-DRC) from the cryo-electro... -
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データベース: EMDB / ID: EMD-20821
タイトル
The Nexin-dynein Regulatory Complex (N-DRC) from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas DRC5-SNAP axonemes, labeled with streptavidin-nanogold
マップデータ
The nexin-dynein regulatory complex averaged from Chlamydomonas DRC5-SNAP axoneme, labeled with streptavidin-nanogold
試料
細胞: The nexin-dynein regulatory complex averaged from Chlamydomonas DRC5-SNAP axoneme, labeled with streptavidin-nanogold
National Institutes of Health/National Institute of General Medical Sciences
R01GM083122
米国
National Institutes of Health/National Institute of General Medical Sciences
R01GM055667
米国
引用
ジャーナル: Proc Natl Acad Sci U S A / 年: 2019 タイトル: Scaffold subunits support associated subunit assembly in the ciliary nexin-dynein regulatory complex. 著者: Long Gui / Kangkang Song / Douglas Tritschler / Raqual Bower / Si Yan / Aguang Dai / Katherine Augspurger / Jason Sakizadeh / Magdalena Grzemska / Thomas Ni / Mary E Porter / Daniela Nicastro / 要旨: The nexin-dynein regulatory complex (N-DRC) in motile cilia and flagella functions as a linker between neighboring doublet microtubules, acts to stabilize the axonemal core structure, and serves as a ...The nexin-dynein regulatory complex (N-DRC) in motile cilia and flagella functions as a linker between neighboring doublet microtubules, acts to stabilize the axonemal core structure, and serves as a central hub for the regulation of ciliary motility. Although the N-DRC has been studied extensively using genetic, biochemical, and structural approaches, the precise arrangement of the 11 (or more) N-DRC subunits remains unknown. Here, using cryo-electron tomography, we have compared the structure of wild-type flagella to that of strains with specific DRC subunit deletions or rescued strains with tagged DRC subunits. Our results show that DRC7 is a central linker subunit that helps connect the N-DRC to the outer dynein arms. DRC11 is required for the assembly of DRC8, and DRC8/11 form a subcomplex in the proximal lobe of the linker domain that is required to form stable contacts to the neighboring B-tubule. Gold labeling of tagged subunits determines the precise locations of the previously ambiguous N terminus of DRC4 and C terminus of DRC5. DRC4 is now shown to contribute to the core scaffold of the N-DRC. Our results reveal the overall architecture of N-DRC, with the 3 subunits DRC1/2/4 forming a core complex that serves as the scaffold for the assembly of the "functional subunits," namely DRC3/5-8/11. These findings shed light on N-DRC assembly and its role in regulating flagellar beating.