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We carried out large-scale transcriptomic and metabolomic analyses to decipher the short-term acclimation of the brown algal model E. siliculosus to Cu stress, and compared these data to results known for other abiotic stressors. This comparison demonstrates that Cu induces oxidative stress in E. siliculosus as illustrated by the transcriptomic overlap between Cu and H2O2 treatments. The common response to Cu and H2O2 consisted in the activation of the oxylipin and the repression of inositol signaling pathways, together with the regulation of genes coding for several transcription-associated proteins. Concomitantly, Cu stress specifically activated a set of genes coding for orthologs of ABC transporters, a P1B-type ATPase, ROS detoxification systems such as a vanadium-dependent bromoperoxidase, and induced an increase of free fatty acid contents. Finally we observed, as a common abiotic stress mechanism, the activation of autophagic processes on one hand and the repression of genes involved in nitrogen assimilation on the other hand.
This study provides an overview of copper stress acclimation in E. siliculosus, and highlights a number of processes that seem to be conserved with metazoans or land plants. Of interest for future brown algal research is the potential cross-talk between ROS, MI, and oxylipin signaling. Considering that two thirds of the regulated genes identified through this work encode proteins of unknown function, many additional components of the stress response remain to be discovered. The number of available medium to high throughput datasets related to stress response in brown algae is still limited , and the analysis of such results paves the way to decipher some of the molecular mechanisms leading to acclimation of these organisms to their frequently changing environment. They will be complemented by follow-up studies benefiting from the development of new techniques and protocols for brown algae, such as reverse genetics (transformation, RNAi, and tilling) or the assessment of nucleic acid-protein and protein-protein interactions. 2b1af7f3a8