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dc.contributor.authorOwa, Mikito
dc.contributor.authorFuruta, Akane
dc.contributor.authorUsukura, Jiro
dc.contributor.authorArisaka, Fumio
dc.contributor.authorKing, Stephen M.
dc.contributor.authorWitman, George B.
dc.contributor.authorKamiya, Ritsu
dc.contributor.authorWakabayashi, Ken-ichi
dc.date2022-08-11T08:08:03.000
dc.date.accessioned2022-08-23T15:40:43Z
dc.date.available2022-08-23T15:40:43Z
dc.date.issued2014-07-01
dc.date.submitted2015-04-01
dc.identifier.citation<p>Proc Natl Acad Sci U S A. 2014 Jul 1;111(26):9461-6. doi: 10.1073/pnas.1403101111. Epub 2014 Jun 16. <a href="http://dx.doi.org/10.1073/pnas.1403101111">Link to article on publisher's site</a></p>
dc.identifier.issn0027-8424 (Linking)
dc.identifier.doi10.1073/pnas.1403101111
dc.identifier.pmid24979786
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26464
dc.description.abstractOuter 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.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=24979786&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rights<p>Publisher PDF posted as allowed by the publisher's author rights policy at http://www.pnas.org/site/aboutpnas/authorfaq.xhtml.</p>
dc.subjectAxoneme
dc.subjectBlotting, Western
dc.subjectChromatography, Gel
dc.subjectDyneins
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectElectroporation
dc.subjectFluorescent Antibody Technique
dc.subjectMacromolecular Substances
dc.subjectMicroscopy, Electron
dc.subjectMicroscopy, Fluorescence
dc.subjectMicrotubules
dc.subject*Models, Biological
dc.subjectProtein Binding
dc.subjectRosaniline Dyes
dc.subjectUltracentrifugation
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectBiochemistry
dc.subjectCell and Developmental Biology
dc.subjectCell Biology
dc.subjectCells
dc.subjectEnzymes and Coenzymes
dc.subjectGenetic Phenomena
dc.subjectInvestigative Techniques
dc.titleCooperative binding of the outer arm-docking complex underlies the regular arrangement of outer arm dynein in the axoneme
dc.typeJournal Article
dc.source.journaltitleProceedings of the National Academy of Sciences of the United States of America
dc.source.volume111
dc.source.issue26
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1148&amp;context=cellbiology_pp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cellbiology_pp/149
dc.identifier.contextkey6929799
refterms.dateFOA2022-08-23T15:40:43Z
html.description.abstract<p>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.</p>
dc.identifier.submissionpathcellbiology_pp/149
dc.contributor.departmentDepartment of Cell and Developmental Biology
dc.source.pages9461-6


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