Function and Regulation of Ferredoxins in the Cyanobacterium, Synechocystis PCC6803: Recent Advances

Life

Corinne Cassier-Chauvat¹  Franck Chauvat²  John C. Meeks² 

[1] UMR8221, CEA, CNRS, Université Paris-Sud, Institut de Biologie et Technologie Saclay, Laboratoire de Biologie et Biotechnologie des Cyanobactéries, CEA-Saclay, Gif sur Yvette 91190, France; E-Mail

关键词: cyanobacteria;    ferredoxins;    iron-sulfur cluster;    electron transfer;    oxidative stress;    metal stress;    regulation;   

DOI  :  10.3390/life4040666

来源: mdpi

【 摘 要 】

Ferredoxins (Fed), occurring in most organisms, are small proteins that use their iron-sulfur cluster to distribute electrons to various metabolic pathways, likely including hydrogen production. Here, we summarize the current knowledge on ferredoxins in cyanobacteria, the prokaryotes regarded as important producers of the oxygenic atmosphere and biomass for the food chain, as well as promising cell factories for biofuel production. Most studies of ferredoxins were performed in the model strain, Synechocystis PCC6803, which possesses nine highly-conserved ferredoxins encoded by monocistronic or operonic genes, some of which are localized in conserved genome regions. Fed1, encoded by a light-inducible gene, is a highly abundant protein essential to photosynthesis. Fed2-Fed9, encoded by genes differently regulated by trophic conditions, are low-abundant proteins that play prominent roles in the tolerance to environmental stresses. Concerning the selectivity/redundancy of ferredoxin, we report that Fed1, Fed7 and Fed9 belong to ferredoxin-glutaredoxin-thioredoxin crosstalk pathways operating in the protection against oxidative and metal stresses. Furthermore, Fed7 specifically interacts with a DnaJ-like protein, an interaction that has been conserved in photosynthetic eukaryotes in the form of a composite protein comprising DnaJ- and Fed7-like domains. Fed9 specifically interacts with the Flv3 flavodiiron protein acting in the photoreduction of O₂ to H₂O.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.