Adaptation of the photosynthetic electron transport chain in cyanobacteria to iron deficiency: The function of IdiA and IsiA
- 6 January 2004
- journal article
- Published by Wiley in Physiologia Plantarum
- Vol. 120 (1) , 36-50
- https://doi.org/10.1111/j.0031-9317.2004.0229.x
Abstract
In this review we give an overview on the adaptational responses of photosystem (PS) II and PSI in cyanobacteria to iron starvation, mainly summarizing our results with the mesophilic Synechococcus elongatus PCC 7942. We also discuss this process with respect to the strong interrelationship between iron limitation and oxidative stress that exists in cyanobacteria as oxygenic photosynthetic organisms. The adaptation of the multiprotein complexes PSII and PSI to iron starvation is a sequential process, which is characterized by the enhanced expression of two major iron‐regulated proteins, IdiA (iron deficiency induced protein A) and IsiA (iron stress induced protein A). Our results suggest that IdiA protects the acceptor side of PSII against oxidative stress under conditions of mild iron limitation in a currently unclear way, whereas prolonged iron deficiency leads to the synthesis of a chlorophyll a antenna around PSI‐trimers consisting of IsiA molecules. The physiological consequences of these alterations under prolonged iron starvation, as shown by acridine yellow fluorescence measurements, are a reduction of linear electron transport activity through PSII and an increase of cyclic electron flow around PSI as well as an increase in respiratory activity. IdiA and IsiA expression are mediated by two distinct helix‐turn‐helix transcriptional regulators of the Crp/Fnr family. IdiB positively regulates expression of idiA under iron starvation, and Fur represses transcription of isiA under iron‐sufficient conditions. Although both transcriptional regulators seem to operate independently of each other, our results indicate that a cross‐talk between the signal transduction pathways exists. Moreover, IdiA as well as IsiA expression are affected by hydrogen peroxide. We suggest that due to the interdependence of iron limitation and the formation of reactive oxygen species, peroxide stress might be the superior trigger that leads to expression of these proteins under iron starvation. The modifications of PSII and PSI under iron starvation influence the redox state of redox‐sensitive components of the electron transport chain, and thus the activity of metabolic pathways being regulated in dependence of the redox state of these components.Keywords
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