Abstract
Thiol/disulfide-based redox regulation is a ubiquitous post-translational protein modification. In plant chloroplasts, this regulatory mechanism is tightly associated with the light-dependent activation of photosynthetic enzymes (e.g. Calvin-Benson cycle enzymes). A thioredoxin (Trx)-mediated pathway was discovered to transmit light signals as a reducing power about half a century ago; since then, it has been accepted as the basic machinery of chloroplast redox regulation. However, during the past two decades, it has been increasingly apparent that plants have acquired multiple Trx isoforms and Trx-like proteins in chloroplasts. Furthermore, proteomics-based analyses have identified various chloroplast enzymes as potential targets of redox regulation. These facts highlight the necessity to revisit the molecular basis and physiological importance of the redox regulation system in chloroplasts. Recent studies have revealed novel aspects of this system, including unprecedented redox-regulated processes in chloroplasts and the functional diversity of Trx family proteins. Of particular significance is the identification of protein-oxidizing pathways that turn off photosynthetic metabolism during light-to-dark transitions. In this review, we summarize current insights into the redox regulation network in chloroplasts.