Volume 67, Issue 3 pp. 243-249
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Motility processes in Acantharia. II. A Ca2+ dependent system of contractile 2–4 nm filaments isolated from demembranated myonemes

Jean Febvre

Corresponding Author

Jean Febvre

Laboratoire de Biologie Cellulaire Marine, UA 671 CNRS, Station Zoologique de Villefranche, CEROV, 06230 Villefranche-sur-Mer, France

Laboratoire de Protistologie Marine UER FST, Nice, Parc Valrose, 06034 Nice Cedex, France

Laboratoire de Biologie Cellulaire Marine, Station Zoologique, 06230 Villefranche-sur-Mer, BP. 28, France.

Laboratoire de Biologie Cellulaire Marine, Station Zoologique, 06230 Villefranche-sur-Mer, BP. 28, France.

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Colette Febvre-Chevalier

Corresponding Author

Colette Febvre-Chevalier

Laboratoire de Biologie Cellulaire Marine, UA 671 CNRS, Station Zoologique de Villefranche, CEROV, 06230 Villefranche-sur-Mer, France

Laboratoire de Protistologie Marine UER FST, Nice, Parc Valrose, 06034 Nice Cedex, France

Laboratoire de Biologie Cellulaire Marine, Station Zoologique, 06230 Villefranche-sur-Mer, BP. 28, France.

Laboratoire de Biologie Cellulaire Marine, Station Zoologique, 06230 Villefranche-sur-Mer, BP. 28, France.

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Abstract

Myonemes of the acantharians are contractile ribbon-like organelles. As previously shown, their motility is based on the coiling mechanism of double-twisted 2–4 nm nonactin filaments [14]. Myonemes have been isolated and manipulated in vitro. After demembranation, the contraction takes place when the Ca2+ concentration is above 10−7 M, whereas relaxation occurs below this threshold concentration. The response to Ca2+ ions is an on/off mechanism. Both contraction and relaxation can be induced repeatedly without fatigue phenomena. Other divalent cations such as Sr2+, Ba2+, Ma2+, CO2+, and La3+ can replace Ca2+ in inducing contraction of the demembranated myonemes although with less efficiency. Contraction and relaxation are ATP-independent and calmodulin is not involved in this in vitro motility process. The myoneme is a strongly resistant structure which is capable of contracting and relaxing under various extreme conditions which indicates very stable proteins and resistant functions.

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