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Thiol switches in redox regulation of chloroplasts: balancing redox state, metabolism and oxidative stress

Karl-Josef Dietz and Rüdiger Hell
From the journal Biological Chemistry


In photosynthesizing chloroplasts, rapidly changing energy input, intermediate generation of strong reductants as well as oxidants and multiple participating physicochemical processes and pathways, call for efficient regulation. Coupling redox information to protein function via thiol modifications offers a powerful mechanism to activate, down-regulate and coordinate interdependent processes. Efficient thiol switching of target proteins involves the thiol-disulfide redox regulatory network, which is highly elaborated in chloroplasts. This review addresses the features of this network. Its conditional function depends on specificity of reduction and oxidation reactions and pathways, thiol redox buffering, but also formation of heterogeneous milieus by microdomains, metabolite gradients and macromolecular assemblies. One major player is glutathione. Its synthesis and function is under feedback redox control. The number of thiol-controlled processes and involved thiol switched proteins is steadily increasing, e.g., in tetrapyrrole biosynthesis, plastid transcription and plastid translation. Thus chloroplasts utilize an intricate and versatile redox regulatory network for intraorganellar and retrograde communication.

Corresponding author: Karl-Josef Dietz, Biochemistry and Physiology of Plants, Faculty of Biology, W5-134, Bielefeld University, University Street 25, D-33501 Bielefeld, Germany, e-mail:


This work was funded by the Deutsche Forschungsgemeinschaft (DFG), in particular within the framework of the Schwerpunktprogramm SPP 1710.


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Received: 2014-11-29
Accepted: 2015-3-2
Published Online: 2015-3-5
Published in Print: 2015-5-1

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