ArticleThe Journal of cell biology1992
The alpha subunit of sea urchin sperm outer arm dynein mediates structural and rigor binding to microtubules.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Turning dyneins off bends cilia.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Torque generation by axonemal outer-arm dynein.Biophysical journal · 2015Article
- Article
- Structural mechanism of the dynein power stroke.Nature cell biology · 2014Article
- Tubulin-dynein system in flagellar and ciliary movement.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2012Review
- A unified taxonomy for ciliary dyneins.Cytoskeleton (Hoboken, N.J.) · 2011Article
- Distinct roles of 1alpha and 1beta heavy chains of the inner arm dynein I1 of Chlamydomonas flagella.Molecular biology of the cell · 2011Article
- Nucleotide-induced global conformational changes of flagellar dynein arms revealed by in situ analysis.Nature structural & molecular biology · 2010Article
- Sensing the mechanical state of the axoneme and integration of Ca2+ signaling by outer arm dynein.Cytoskeleton (Hoboken, N.J.) · 2010Review
- Article
- Dynein pulls microtubules without rotating its stalk.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Partially functional outer-arm dynein in a novel Chlamydomonas mutant expressing a truncated gamma heavy chain.Eukaryotic cell · 2008Article
- 3D structure of eukaryotic flagella in a quiescent state revealed by cryo-electron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- The Chlamydomonas reinhardtii ODA3 gene encodes a protein of the outer dynein arm docking complex.The Journal of cell biology · 1997Article
- Is outer arm dynein intermediate chain 1 multifunctional?Molecular biology of the cell · 1996Article
- The 78,000-M(r) intermediate chain of Chlamydomonas outer arm dynein is a microtubule-binding protein.The Journal of cell biology · 1995Article
- Interspecies conservation of outer arm dynein intermediate chain sequences defines two intermediate chain subclasses.Molecular biology of the cell · 1995Article
- A Chlamydomonas outer arm dynein mutant with a truncated beta heavy chain.The Journal of cell biology · 1993Article
- The motile beta/IC1 subunit of sea urchin sperm outer arm dynein does not form a rigor bond.The Journal of cell biology · 1992Article
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Authors and funding
4 authors.
Funding
Abstract
Glass-adsorbed intact sea urchin outer arm dynein and its beta/IC1 subunit supports movement of microtubules, yet does not form a rigor complex upon depletion of ATP (16). We show here that rigor is a feature of the isolated intact outer arm, and that this property subfractionates with its alpha heavy chain. Intact dynein mediates the formation of ATP-sensitive microtubule bundles, as does the purified alpha heavy chain, indicating that both particles are capable of binding to microtubules in an ATP-sensitive manner. In contrast, the beta/IC1 subunit does not bundle microtubules. Bundles formed with intact dynein are composed of ribbon-like sheets of parallel microtubules that are separated by 54 nm (center-to-center) and display the same longitudinal repeat (24 nm) and cross-sectional geometry of dynein arms as do outer doublets in situ. Bundles formed by the alpha heavy chain are composed of microtubules with a center-to-center spacing of 43 nm and display infrequent, fine crossbridges. In contrast to the bridges formed by the intact arm, the links formed by the alpha subunit are irregularly spaced, suggesting that binding of the alpha heavy chain to the microtubules is not cooperative. Cosedimentation studies showed that: (a) some of the intact dynein binds in an ATP-dependent manner and some binds in an ATP-independent manner; (b) the beta/IC1 subunit does not cosediment with microtubules under any conditions; and (c) the alpha heavy chain cosediments with microtubules in the absence or presence of MgATP2-. These results suggest that the structural binding observed in the intact arm also is a property of its alpha heavy chain. We conclude that whereas force-generation is a function of the beta/IC1 subunit, both structural and ATP-sensitive (rigor) binding of the arm to the microtubule are mediated by the alpha subunit.
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