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ATP-dependent structural changes of the outer dynein arm in Tetrahymena cilia: a freeze-etch replica study

With the rapid-freeze, deep-etch replica technique, the structural conformations of outer dynein arms in demembranated cilia from Tetrahymena were analyzed under two different conditions, i.e., in the absence of ATP and in the presence of ATP and vanadate. In the absence of ATP, the lateral view of...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1983
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112665/
https://www.ncbi.nlm.nih.gov/pubmed/6221024
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description With the rapid-freeze, deep-etch replica technique, the structural conformations of outer dynein arms in demembranated cilia from Tetrahymena were analyzed under two different conditions, i.e., in the absence of ATP and in the presence of ATP and vanadate. In the absence of ATP, the lateral view of axonemes was characterized by the egg- shaped outer dynein arms, which showed a slightly baseward tilt with a mean inclination of 11.1 degrees +/- 3.4 degrees SD from the perpendicular to the doublet microtubules. On the other hand, in the presence of 1 mM ATP and 100 microM vanadate, the outer arms were extended and slender and showed an increased baseward tilt with a mean inclination of 31.6 degrees +/- 4.9 degrees SD. In ATP-activated axonemes, these two types of arms coexisted, each type occurring in groups along one row of outer arms. These findings strongly suggest that the interdoublet sliding is caused by dynamic structural changes of dynein arms that follow the hydrolysis of ATP.
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spelling pubmed-21126652008-05-01 ATP-dependent structural changes of the outer dynein arm in Tetrahymena cilia: a freeze-etch replica study J Cell Biol Articles With the rapid-freeze, deep-etch replica technique, the structural conformations of outer dynein arms in demembranated cilia from Tetrahymena were analyzed under two different conditions, i.e., in the absence of ATP and in the presence of ATP and vanadate. In the absence of ATP, the lateral view of axonemes was characterized by the egg- shaped outer dynein arms, which showed a slightly baseward tilt with a mean inclination of 11.1 degrees +/- 3.4 degrees SD from the perpendicular to the doublet microtubules. On the other hand, in the presence of 1 mM ATP and 100 microM vanadate, the outer arms were extended and slender and showed an increased baseward tilt with a mean inclination of 31.6 degrees +/- 4.9 degrees SD. In ATP-activated axonemes, these two types of arms coexisted, each type occurring in groups along one row of outer arms. These findings strongly suggest that the interdoublet sliding is caused by dynamic structural changes of dynein arms that follow the hydrolysis of ATP. The Rockefeller University Press 1983-05-01 /pmc/articles/PMC2112665/ /pubmed/6221024 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
ATP-dependent structural changes of the outer dynein arm in Tetrahymena cilia: a freeze-etch replica study
title ATP-dependent structural changes of the outer dynein arm in Tetrahymena cilia: a freeze-etch replica study
title_full ATP-dependent structural changes of the outer dynein arm in Tetrahymena cilia: a freeze-etch replica study
title_fullStr ATP-dependent structural changes of the outer dynein arm in Tetrahymena cilia: a freeze-etch replica study
title_full_unstemmed ATP-dependent structural changes of the outer dynein arm in Tetrahymena cilia: a freeze-etch replica study
title_short ATP-dependent structural changes of the outer dynein arm in Tetrahymena cilia: a freeze-etch replica study
title_sort atp-dependent structural changes of the outer dynein arm in tetrahymena cilia: a freeze-etch replica study
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2112665/
https://www.ncbi.nlm.nih.gov/pubmed/6221024