The Outer Dynein Arm-Docking Complex: Composition and Characterization of a Subunit (Oda1) Necessary for Outer Arm Assembly

Takada, Saeko; Wilkerson, Curtis G.; Wakabayashi, K.; Kamiya, Ritsu; Witman, George B.

doi:10.1091/mbc.01-04-0201

Cited by 122 publications

(140 citation statements)

References 48 publications

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“…Flagellar beat frequency was determined as described previously (Kamiya, 2000). Kamiya, 1988;Takada et al, 2002ODA2 ␥DHC Kamiya, 1988Mitchell and Rosenbaum, 1985;Wilkerson et al, 1994ODA3 DC1 Kamiya, 1988Koutoulis et al, 1997ODA4 ␤DHC Kamiya, 1988Mitchell and Brown, 1994;Sakakibara et al, 1993 ODA5 This study Kamiya, 1988ODA6 IC2 Kamiya, 1988Mitchell and Kang, 1991ODA7 ? Kamiya, 1988ODA8 ?…”

Section: Motion Analysismentioning

confidence: 99%

“…Demembranated axonemes were subsequently extracted with 0.6 M KCl in HMDEKP buffer. High-salt extracts were fractionated on 5-20% sucrose gradients under conditions that maintain the association of the outer arm and the ODA-DC (Takada et al, 2002). A mixture of bovine thyroglobulin, catalase, and bovine serum albumin (Sigma-Aldrich) was run in a parallel gradient for S-value determination.…”

Section: Isolation Of Flagella and Flagellar Fractionationsmentioning

confidence: 99%

“…Previous data have shown that the outer arm and the ODA-DC also are released from the axoneme by 0.6 M KCl (Pfister et al, 1982;Takada et al, 1992;Takada et al, 2002). To determine whether Oda5p associates with the outer arm or the ODA-DC, we subjected the high-salt extract to sucrose gradient sedimentation, by using conditions designed to maintain the outer arm/ODA-DC association (Takada et al, 1992).…”

Section: Oda5p Is An Axonemal Proteinmentioning

confidence: 99%

“…Western blots ( Figure 6A) revealed that Oda5p is present in axonemes of an oda9 mutant, which is defective in the IC1 gene and fails to assemble an outer arm (Wilkerson et al, 1995), and of oda1 and oda3 mutants, which are defective in the DC2 and DC1 components of the docking complex, respectively (Koutoulis et al, 1997;Takada et al, 2002) and fail to assemble the ODA-DC and the outer arm. These results show that Oda5p can assemble onto the axoneme independently of the outer arm and the ODA-DC.…”

Section: Oda5p Assembles Onto the Axoneme Independently Of The Outer mentioning

confidence: 99%

“…The correct positioning of the outer arm is due at least in part to its association with the outer dynein arm-docking complex (ODA-DC), which is required for attachment of the outer arm onto the A-tubule. The ODA-DC, a heterotrimeric complex comprised of subunits DC1 (Koutoulis et al, 1997), DC2 (Takada et al, 2002), and DC3 (Casey et al, 2003), assembles onto the site normally occupied by the outer arm even in the absence of the latter structure.…”

Section: Introductionmentioning

confidence: 99%

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Oda5p, a Novel Axonemal Protein Required for Assembly of the Outer Dynein Arm and an Associated Adenylate Kinase

Wirschell

Pazour

Yoda

et al. 2004

MBoC

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Of the uncloned ODA genes required for outer dynein arm assembly in Chlamydomonas, ODA5 and ODA10 are of particular interest because they do not encode known subunits of the outer arm or the outer dynein arm-docking complex (ODA-DC), and because genetic studies suggest their products interact. Beginning with a tagged oda5 allele, we isolated genomic and cDNA clones of the wild-type gene. ODA5 predicts a novel, 66-kDa coiled-coil protein. Immunoblotting indicates Oda5p is an axonemal component that assembles onto the axoneme independently of the outer arm and ODA-DC and is uniquely missing in oda5 and oda10 axonemes. Oda5p is released from the axoneme by extraction with 0.6 M KCl, but the soluble Oda5p does not cosediment with the outer dynein arm/ODA-DC in sucrose gradients. Quantitative mass spectrometry by using isotope coded affinity tagging revealed that a previously unidentified adenylate kinase is reduced 35-50% in oda5 flagella. Direct enzymatic assays demonstrated a comparable reduction in adenylate kinase activity in oda5 flagella, and also in oda10 flagella, but not in flagella of other oda mutants. We propose that Oda5p is part of a novel axonemal complex that is required for outer arm assembly and anchors adenylate kinase in proximity to the arm.

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Section: Motion Analysismentioning

confidence: 99%

Section: Isolation Of Flagella and Flagellar Fractionationsmentioning

confidence: 99%

Section: Oda5p Is An Axonemal Proteinmentioning

confidence: 99%

Section: Oda5p Assembles Onto the Axoneme Independently Of The Outer mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Oda5p, a Novel Axonemal Protein Required for Assembly of the Outer Dynein Arm and an Associated Adenylate Kinase

Wirschell

Pazour

Yoda

et al. 2004

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Algal Flagella

Wirschell

Dutcher

2011

Encyclopedia of Life Sciences

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Flagella are highly conserved organelles comprised of several hundred proteins that are assembled using the equally conserved mechanism called intraflagellar transport (IFT). The molecular motors dynein and kinesin drive IFT‐mediated flagellar assembly. In addition, flagellar movement is powered by the flagellar dynein motors. The outer and inner dynein arms function in generating flagellar beat frequency and flagellar waveform that are the two main features of flagellar bending. The biflagellate algae Chlamydomonas reinhardtii is a powerful model organism for the study of flagellar assembly and function. Recent advances have revealed that cilia and flagella play vital motile and sensory roles in the developing human embryo and in adult tissue function. Defects in assembly or function of mammalian cilia/flagella underlie an expanding set of human diseases and syndromes, collectively called ‘the ciliopathies’. Much of our current understanding of flagellar assembly, motility and the ciliopathies has come from studies in Chlamydomonas . Key Concepts: Cilia and flagella are highly conserved organelles. Dynein motors drive flagellar movement. Chlamydomonas reinhardtii is a powerful model experimental system for studying flagella. Defects in assembly or function of cilia/flagella result in multiple pathologies called ‘the ciliopathies’.

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Does axonemal dynein push, pull, or oscillate?

Lindemann

Hunt

2003

Cell Motil. Cytoskeleton

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Dynein is the molecular motor that provides motive force in cilia and flagella. Dynein is anchored to the A-subtubule of the outer doublets by a club-shaped extension called the stem, which supports the large globular head of the molecule. Dynein forms an attachment or cross-bridge to the B-subtubule of the adjacent outer doublet through a slender appendage extending from the head that is called the stalk or alternately the B-link. It is generally thought that the B-link mediates the interdoublet transfer of force that bends the flagellum. This requires that energy released at the site of ATP hydrolysis, located in the globular head, be transferred as mechanical work to the microtubule binding site at the tip of the B-link. It has been proposed that this is accomplished by a sideways or rotational translocation of the B-link caused by a rotation of the globular head. An estimate of the stiffness of the B-link and stem derived from the recently published data of Burgess et al. [2003: Nature 421:715-718] yields a maximum stiffness of 0.47 pN/nm for the B-link and 0.1 pN/nm for the stem. The B-link stiffness would allow transfer of 3.8 pN of force in response to an 8-nm displacement of the B-link tip. However, if as proposed the globular head of the dynein heavy chain is supported by the stem, the B-link and stem elasticity are in series. Thus, the flexibility of the stem would limit the force that can be transferred laterally by the entire dynein heavy chain to 0.6 pN at 8 nm displacement. This force is insufficient to support flagellar motility. So, if the stem were the only support for the globular head, then force would have to be transmitted linearly along the axis defined by the stem and B-link. Because this configuration is never observed, the hypothesis that dynein generates force by lateral displacement of the B-link is more attractive, but requires that the globular head of the dynein is stabilized by an additional means of support during the power stroke. We propose that the microtubule affinity of the tip of the B-link is independent of the ATP-dependent powerstroke, and that detachment from the B-subtubule is regulated by tension. A dynein cross-bridge cycle that incorporates an anchored head, together with a ratchet-like mechanism for microtubule translocation by the B-link, would have distinct advantages. This mechanism may reconcile dynein oscillation and interdoublet sliding within one cross-bridge mechanism. Cell Motil. Cytoskeleton 56: 237-244, 2003.

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The Outer Dynein Arm-Docking Complex: Composition and Characterization of a Subunit (Oda1) Necessary for Outer Arm Assembly

Cited by 122 publications

References 48 publications

Oda5p, a Novel Axonemal Protein Required for Assembly of the Outer Dynein Arm and an Associated Adenylate Kinase

Oda5p, a Novel Axonemal Protein Required for Assembly of the Outer Dynein Arm and an Associated Adenylate Kinase

Algal Flagella

Does axonemal dynein push, pull, or oscillate?

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