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Structure and function of outer dynein arm intermediate and light chain complex
The outer dynein arm (ODA) is a molecular complex that drives the beating motion of cilia/flagella. Chlamydomonas ODA is composed of three heavy chains (HCs), two ICs, and 11 light chains (LCs). Although the three-dimensional (3D) structure of the whole ODA complex has been investigated, the 3D conf...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4814214/ https://www.ncbi.nlm.nih.gov/pubmed/26864626 http://dx.doi.org/10.1091/mbc.E15-10-0723 |
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author | Oda, Toshiyuki Abe, Tatsuki Yanagisawa, Haruaki Kikkawa, Masahide |
author_facet | Oda, Toshiyuki Abe, Tatsuki Yanagisawa, Haruaki Kikkawa, Masahide |
author_sort | Oda, Toshiyuki |
collection | PubMed |
description | The outer dynein arm (ODA) is a molecular complex that drives the beating motion of cilia/flagella. Chlamydomonas ODA is composed of three heavy chains (HCs), two ICs, and 11 light chains (LCs). Although the three-dimensional (3D) structure of the whole ODA complex has been investigated, the 3D configurations of the ICs and LCs are largely unknown. Here we identified the 3D positions of the two ICs and three LCs using cryo–electron tomography and structural labeling. 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. Of interest, the coiled-coil domain of IC2 extended from the ODA-Beak to the outer surface of ODA. Furthermore, we investigated the molecular mechanisms of how the OID linker transmits signals to the ODA-Beak, by manipulating the interaction within the OID linker using a chemically induced dimerization system. 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. |
format | Online Article Text |
id | pubmed-4814214 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-48142142016-06-16 Structure and function of outer dynein arm intermediate and light chain complex Oda, Toshiyuki Abe, Tatsuki Yanagisawa, Haruaki Kikkawa, Masahide Mol Biol Cell Brief Report The outer dynein arm (ODA) is a molecular complex that drives the beating motion of cilia/flagella. Chlamydomonas ODA is composed of three heavy chains (HCs), two ICs, and 11 light chains (LCs). Although the three-dimensional (3D) structure of the whole ODA complex has been investigated, the 3D configurations of the ICs and LCs are largely unknown. Here we identified the 3D positions of the two ICs and three LCs using cryo–electron tomography and structural labeling. 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. Of interest, the coiled-coil domain of IC2 extended from the ODA-Beak to the outer surface of ODA. Furthermore, we investigated the molecular mechanisms of how the OID linker transmits signals to the ODA-Beak, by manipulating the interaction within the OID linker using a chemically induced dimerization system. 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. The American Society for Cell Biology 2016-04-01 /pmc/articles/PMC4814214/ /pubmed/26864626 http://dx.doi.org/10.1091/mbc.E15-10-0723 Text en © 2016 Oda et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Brief Report Oda, Toshiyuki Abe, Tatsuki Yanagisawa, Haruaki Kikkawa, Masahide Structure and function of outer dynein arm intermediate and light chain complex |
title | Structure and function of outer dynein arm intermediate and light chain complex |
title_full | Structure and function of outer dynein arm intermediate and light chain complex |
title_fullStr | Structure and function of outer dynein arm intermediate and light chain complex |
title_full_unstemmed | Structure and function of outer dynein arm intermediate and light chain complex |
title_short | Structure and function of outer dynein arm intermediate and light chain complex |
title_sort | structure and function of outer dynein arm intermediate and light chain complex |
topic | Brief Report |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4814214/ https://www.ncbi.nlm.nih.gov/pubmed/26864626 http://dx.doi.org/10.1091/mbc.E15-10-0723 |
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