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Calredoxin represents a novel type of calcium-dependent sensor-responder connected to redox regulation in the chloroplast

Author

Listed:
  • Ana Karina Hochmal

    (Institute of Plant Biology and Biotechnology, University of Münster)

  • Karen Zinzius

    (Institute of Plant Biology and Biotechnology, University of Münster)

  • Ratana Charoenwattanasatien

    (Institute for Protein Research, Osaka University)

  • Philipp Gäbelein

    (Institute of Plant Biology and Biotechnology, University of Münster)

  • Risa Mutoh

    (Institute for Protein Research, Osaka University
    Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST))

  • Hideaki Tanaka

    (Institute for Protein Research, Osaka University
    Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST))

  • Stefan Schulze

    (Institute of Plant Biology and Biotechnology, University of Münster)

  • Gai Liu

    (Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences)

  • Martin Scholz

    (Institute of Plant Biology and Biotechnology, University of Münster)

  • André Nordhues

    (Institute of Plant Biology and Biotechnology, University of Münster)

  • Jan Niklas Offenborn

    (Institute of Plant Biology and Biotechnology, University of Münster)

  • Dimitris Petroutsos

    (Centre National Recherche Scientifique, Unité Mixte Recherche 5168, Laboratoire Physiologie Cellulaire et Végétale
    Commissariat à l'Energie Atomique et Energies Alternatives, l'Institut de Recherches en Technologies et Sciences pour le Vivant
    Université Grenoble 1
    Institut National Recherche Agronomique, UMR1200)

  • Giovanni Finazzi

    (Centre National Recherche Scientifique, Unité Mixte Recherche 5168, Laboratoire Physiologie Cellulaire et Végétale
    Commissariat à l'Energie Atomique et Energies Alternatives, l'Institut de Recherches en Technologies et Sciences pour le Vivant
    Université Grenoble 1
    Institut National Recherche Agronomique, UMR1200)

  • Christian Fufezan

    (Institute of Plant Biology and Biotechnology, University of Münster)

  • Kaiyao Huang

    (Key Laboratory of Algal Biology, Institute of Hydrobiology, Chinese Academy of Sciences)

  • Genji Kurisu

    (Institute for Protein Research, Osaka University
    Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Agency (JST))

  • Michael Hippler

    (Institute of Plant Biology and Biotechnology, University of Münster)

Abstract

Calcium (Ca2+) and redox signalling play important roles in acclimation processes from archaea to eukaryotic organisms. Herein we characterized a unique protein from Chlamydomonas reinhardtii that has the competence to integrate Ca2+- and redox-related signalling. This protein, designated as calredoxin (CRX), combines four Ca2+-binding EF-hands and a thioredoxin (TRX) domain. A crystal structure of CRX, at 1.6 Å resolution, revealed an unusual calmodulin-fold of the Ca2+-binding EF-hands, which is functionally linked via an inter-domain communication path with the enzymatically active TRX domain. CRX is chloroplast-localized and interacted with a chloroplast 2-Cys peroxiredoxin (PRX1). Ca2+-binding to CRX is critical for its TRX activity and for efficient binding and reduction of PRX1. Thereby, CRX represents a new class of Ca2+-dependent ‘sensor-responder’ proteins. Genetically engineered Chlamydomonas strains with strongly diminished amounts of CRX revealed altered photosynthetic electron transfer and were affected in oxidative stress response underpinning a function of CRX in stress acclimation.

Suggested Citation

  • Ana Karina Hochmal & Karen Zinzius & Ratana Charoenwattanasatien & Philipp Gäbelein & Risa Mutoh & Hideaki Tanaka & Stefan Schulze & Gai Liu & Martin Scholz & André Nordhues & Jan Niklas Offenborn & D, 2016. "Calredoxin represents a novel type of calcium-dependent sensor-responder connected to redox regulation in the chloroplast," Nature Communications, Nature, vol. 7(1), pages 1-14, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11847
    DOI: 10.1038/ncomms11847
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