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Structure and function of outer dynein arm intermediate and light chain complex.

Oda T, Abe T, Yanagisawa H, Kikkawa M - Mol. Biol. Cell (2016)

Bottom Line: We found that these ICs and LCs were all localized at the root of the outer-inner dynein (OID) linker, designated the ODA-Beak complex.We showed that the cross-linking of the OID linker strongly suppresses flagellar motility in vivo.These results suggest that the ICs and LCs of the ODA form the ODA-Beak, which may be involved in mechanosignaling from the OID linker to the HCs.

View Article: PubMed Central - PubMed

Affiliation: Department of Cell Biology and Anatomy, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan Department of Anatomy and Structural Biology, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Chuo, Yamanashi 409-3898, Japan toda@yamanashi.ac.jp.

No MeSH data available.


Related in: MedlinePlus

Structural labeling of ICs and LCs. (A) The 3D structures of the axoneme. Left, tip-to-base view of the 9+2 structure. Right, enlarged view of one of the DMTs. The 90°-rotated views of the DMT are shown on the left of B. (B) The 3D localizations of the labels on ICs and LCs. Arrowheads indicate positions of slices on the right. Colored densities indicate positions of streptavidin labels. Colors of the label densities correspond to colors of arrowheads in Figure 1A. Position of IC2-M549 differed from that in our previous result (Oda et al., 2013). We believe that our previous localization of the C-terminus of IC2 was an artifact due to flexibility of the ODA–microtubule complex. N-DRC and IC-LC complex of IDA f are indicated (gray). (C, D) Structural configuration of ODA and N-DRC. (C) Approximate positions of α, β, and γ HCs (orange) based on previous reports (Nicastro et al., 2006; Ishikawa et al., 2007; Oda et al., 2007; Movassagh et al., 2010; Ueno et al., 2012; Lin et al., 2014). Ovals and lines indicate head and tail domains of HCs, respectively. Arrowhead indicates one of the OID linkers (OID linker 3a) bridging between ODA and N-DRC (pink). (D) Possible 3D configuration of ICs and LCs. Red structure represents IC2, composed of WD repeat (yellow frustum) and coiled-coil (yellow rod). Yellow structure behind IC2 represents IC1, composed of WD repeat (red frustum) and the N-terminal domain (red rod). Three small ovals below IC2 represent LCs. (C, D) ICs and LCs form the ODA-Beak complexes (green). (E) Diagram modified from Figure 2a of Goodenough and Heuser (1984), showing the bouquet structure of the isolated ODA. Annotations of subunits were taken from the same figure, except for assignments of the α, β, and γ HCs.
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Figure 2: Structural labeling of ICs and LCs. (A) The 3D structures of the axoneme. Left, tip-to-base view of the 9+2 structure. Right, enlarged view of one of the DMTs. The 90°-rotated views of the DMT are shown on the left of B. (B) The 3D localizations of the labels on ICs and LCs. Arrowheads indicate positions of slices on the right. Colored densities indicate positions of streptavidin labels. Colors of the label densities correspond to colors of arrowheads in Figure 1A. Position of IC2-M549 differed from that in our previous result (Oda et al., 2013). We believe that our previous localization of the C-terminus of IC2 was an artifact due to flexibility of the ODA–microtubule complex. N-DRC and IC-LC complex of IDA f are indicated (gray). (C, D) Structural configuration of ODA and N-DRC. (C) Approximate positions of α, β, and γ HCs (orange) based on previous reports (Nicastro et al., 2006; Ishikawa et al., 2007; Oda et al., 2007; Movassagh et al., 2010; Ueno et al., 2012; Lin et al., 2014). Ovals and lines indicate head and tail domains of HCs, respectively. Arrowhead indicates one of the OID linkers (OID linker 3a) bridging between ODA and N-DRC (pink). (D) Possible 3D configuration of ICs and LCs. Red structure represents IC2, composed of WD repeat (yellow frustum) and coiled-coil (yellow rod). Yellow structure behind IC2 represents IC1, composed of WD repeat (red frustum) and the N-terminal domain (red rod). Three small ovals below IC2 represent LCs. (C, D) ICs and LCs form the ODA-Beak complexes (green). (E) Diagram modified from Figure 2a of Goodenough and Heuser (1984), showing the bouquet structure of the isolated ODA. Annotations of subunits were taken from the same figure, except for assignments of the α, β, and γ HCs.

Mentions: BCCP-tagging of ICs and LCs. (A) Domain organization of ICs and LCs. Arrowheads indicate positions of BCCP tags. Numbers indicate amino acid residues. Both IC1 and IC2 have WD repeat domains (WD), and the C-terminal domain of IC2 is predicted to form a coiled-coil (Lupas et al., 1991). Colors of arrowheads correspond to colors of label densities in Figure 2B. (B) Immunoblots of axonemal proteins separated by SDS–PAGE and probed with various antibodies. All BCCP-tagged proteins were properly expressed and biotinylated.


Structure and function of outer dynein arm intermediate and light chain complex.

Oda T, Abe T, Yanagisawa H, Kikkawa M - Mol. Biol. Cell (2016)

Structural labeling of ICs and LCs. (A) The 3D structures of the axoneme. Left, tip-to-base view of the 9+2 structure. Right, enlarged view of one of the DMTs. The 90°-rotated views of the DMT are shown on the left of B. (B) The 3D localizations of the labels on ICs and LCs. Arrowheads indicate positions of slices on the right. Colored densities indicate positions of streptavidin labels. Colors of the label densities correspond to colors of arrowheads in Figure 1A. Position of IC2-M549 differed from that in our previous result (Oda et al., 2013). We believe that our previous localization of the C-terminus of IC2 was an artifact due to flexibility of the ODA–microtubule complex. N-DRC and IC-LC complex of IDA f are indicated (gray). (C, D) Structural configuration of ODA and N-DRC. (C) Approximate positions of α, β, and γ HCs (orange) based on previous reports (Nicastro et al., 2006; Ishikawa et al., 2007; Oda et al., 2007; Movassagh et al., 2010; Ueno et al., 2012; Lin et al., 2014). Ovals and lines indicate head and tail domains of HCs, respectively. Arrowhead indicates one of the OID linkers (OID linker 3a) bridging between ODA and N-DRC (pink). (D) Possible 3D configuration of ICs and LCs. Red structure represents IC2, composed of WD repeat (yellow frustum) and coiled-coil (yellow rod). Yellow structure behind IC2 represents IC1, composed of WD repeat (red frustum) and the N-terminal domain (red rod). Three small ovals below IC2 represent LCs. (C, D) ICs and LCs form the ODA-Beak complexes (green). (E) Diagram modified from Figure 2a of Goodenough and Heuser (1984), showing the bouquet structure of the isolated ODA. Annotations of subunits were taken from the same figure, except for assignments of the α, β, and γ HCs.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4814214&req=5

Figure 2: Structural labeling of ICs and LCs. (A) The 3D structures of the axoneme. Left, tip-to-base view of the 9+2 structure. Right, enlarged view of one of the DMTs. The 90°-rotated views of the DMT are shown on the left of B. (B) The 3D localizations of the labels on ICs and LCs. Arrowheads indicate positions of slices on the right. Colored densities indicate positions of streptavidin labels. Colors of the label densities correspond to colors of arrowheads in Figure 1A. Position of IC2-M549 differed from that in our previous result (Oda et al., 2013). We believe that our previous localization of the C-terminus of IC2 was an artifact due to flexibility of the ODA–microtubule complex. N-DRC and IC-LC complex of IDA f are indicated (gray). (C, D) Structural configuration of ODA and N-DRC. (C) Approximate positions of α, β, and γ HCs (orange) based on previous reports (Nicastro et al., 2006; Ishikawa et al., 2007; Oda et al., 2007; Movassagh et al., 2010; Ueno et al., 2012; Lin et al., 2014). Ovals and lines indicate head and tail domains of HCs, respectively. Arrowhead indicates one of the OID linkers (OID linker 3a) bridging between ODA and N-DRC (pink). (D) Possible 3D configuration of ICs and LCs. Red structure represents IC2, composed of WD repeat (yellow frustum) and coiled-coil (yellow rod). Yellow structure behind IC2 represents IC1, composed of WD repeat (red frustum) and the N-terminal domain (red rod). Three small ovals below IC2 represent LCs. (C, D) ICs and LCs form the ODA-Beak complexes (green). (E) Diagram modified from Figure 2a of Goodenough and Heuser (1984), showing the bouquet structure of the isolated ODA. Annotations of subunits were taken from the same figure, except for assignments of the α, β, and γ HCs.
Mentions: BCCP-tagging of ICs and LCs. (A) Domain organization of ICs and LCs. Arrowheads indicate positions of BCCP tags. Numbers indicate amino acid residues. Both IC1 and IC2 have WD repeat domains (WD), and the C-terminal domain of IC2 is predicted to form a coiled-coil (Lupas et al., 1991). Colors of arrowheads correspond to colors of label densities in Figure 2B. (B) Immunoblots of axonemal proteins separated by SDS–PAGE and probed with various antibodies. All BCCP-tagged proteins were properly expressed and biotinylated.

Bottom Line: We found that these ICs and LCs were all localized at the root of the outer-inner dynein (OID) linker, designated the ODA-Beak complex.We showed that the cross-linking of the OID linker strongly suppresses flagellar motility in vivo.These results suggest that the ICs and LCs of the ODA form the ODA-Beak, which may be involved in mechanosignaling from the OID linker to the HCs.

View Article: PubMed Central - PubMed

Affiliation: Department of Cell Biology and Anatomy, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan Department of Anatomy and Structural Biology, Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, Chuo, Yamanashi 409-3898, Japan toda@yamanashi.ac.jp.

No MeSH data available.


Related in: MedlinePlus