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

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 angstrom 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.
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Ana Karina Hochmal, Karen Zinzius, Ratana Charoenwattanasatien, Philipp Gäbelein, Risa Mutoh, et al.. Calredoxin represents a novel type of calcium-dependent sensor-responder connected to redox regulation in the chloroplast. Nature Communications, Nature Publishing Group, 2016, 7, pp.11847. ⟨10.1038/ncomms11847⟩. ⟨hal-01412644⟩

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