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Identification of calmodulin in the green alga Mougeotia and its possible function in chloroplast reorientational movement

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Abstract

A soluble protein was isolated from Mougeotia by chloropromazine-sepharose 4 B affinity chromatography. The protein matches the properties of calmodulin in terms of heat stability, Ca2+-dependent electrophoretic mobility in sodium-dodecyl-sulfate polyacrylamide gels, and its ability to activate cyclic nucleotide phosphodiesterase in a Ca2+-dependent manner. Phytochrome-mediated chloroplast reorientational movement in Mougeotia was inhibited by the calmodulin antagonist trifluoperazine, a hydrophobic compound, or N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7), a hydrophilic compound; 50% inhibition (IC50) of chloroplast movement is caused by 20–50 μmol l-1 trifluoperazine or 100 μmol l-1 W-7. The Ca2+-calmodulin may act as an intermediate in the chloroplast reorientational response in Mougeotia governed by phytochrome.

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Abbreviations

EGTA:

ethylene glycol-bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid

SDS:

sodium dodecyl sulfate

W-7:

N-(6-aminohexyl)-5-chloro-1-naphthalene sulfonamide

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Authors and Affiliations

  1. Botanisches Institut I der Justus-Liebig-Universität, Senckenbergstrasse 17-21, D-6300, Giessen, Germany

    Gottfried Wagner & Petra Valentin

  2. Institut für Biologie III der Universität, Schänzlestrasse 1, D-7800, Freiburg i. Br., Germany

    Peter Dieter & Dieter Marmé

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  1. Gottfried Wagner
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  2. Petra Valentin
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  3. Peter Dieter
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  4. Dieter Marmé
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Wagner, G., Valentin, P., Dieter, P. et al. Identification of calmodulin in the green alga Mougeotia and its possible function in chloroplast reorientational movement. Planta 162, 62–67 (1984). https://doi.org/10.1007/BF00397422

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  • DOI: https://doi.org/10.1007/BF00397422

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