Cooperative binding of the outer arm-docking complex underlies the regular arrangement of outer arm dynein in the axoneme
Authors
Owa, MikitoFuruta, Akane
Usukura, Jiro
Arisaka, Fumio
King, Stephen M.
Witman, George B.
Kamiya, Ritsu
Wakabayashi, Ken-ichi
UMass Chan Affiliations
Department of Cell and Developmental BiologyDocument Type
Journal ArticlePublication Date
2014-07-01Keywords
AxonemeBlotting, Western
Chromatography, Gel
Dyneins
Electrophoresis, Polyacrylamide Gel
Electroporation
Fluorescent Antibody Technique
Macromolecular Substances
Microscopy, Electron
Microscopy, Fluorescence
Microtubules
*Models, Biological
Protein Binding
Rosaniline Dyes
Ultracentrifugation
Amino Acids, Peptides, and Proteins
Biochemistry
Cell and Developmental Biology
Cell Biology
Cells
Enzymes and Coenzymes
Genetic Phenomena
Investigative Techniques
Metadata
Show full item recordAbstract
Outer arm dynein (OAD) in cilia and flagella is bound to the outer doublet microtubules every 24 nm. Periodic binding of OADs at specific sites is important for efficient cilia/flagella beating; however, the molecular mechanism that specifies OAD arrangement remains elusive. Studies using the green alga Chlamydomonas reinhardtii have shown that the OAD-docking complex (ODA-DC), a heterotrimeric complex present at the OAD base, functions as the OAD docking site on the doublet. We find that the ODA-DC has an ellipsoidal shape approximately 24 nm in length. In mutant axonemes that lack OAD but retain the ODA-DC, ODA-DC molecules are aligned in an end-to-end manner along the outer doublets. When flagella of a mutant lacking ODA-DCs are supplied with ODA-DCs upon gamete fusion, ODA-DC molecules first bind to the mutant axonemes in the proximal region, and the occupied region gradually extends toward the tip, followed by binding of OADs. This and other results indicate that a cooperative association of the ODA-DC underlies its function as the OAD-docking site and is the determinant of the 24-nm periodicity.Source
Proc Natl Acad Sci U S A. 2014 Jul 1;111(26):9461-6. doi: 10.1073/pnas.1403101111. Epub 2014 Jun 16. Link to article on publisher's site
DOI
10.1073/pnas.1403101111Permanent Link to this Item
http://hdl.handle.net/20.500.14038/26464PubMed ID
24979786Related Resources
Rights
Publisher PDF posted as allowed by the publisher's author rights policy at http://www.pnas.org/site/aboutpnas/authorfaq.xhtml.
ae974a485f413a2113503eed53cd6c53
10.1073/pnas.1403101111