ACONITASE 3 is part of theANAC017 transcription factor-dependent mitochondrial dysfunction response.

Mitochondria are tightly embedded within metabolic and regulatory networks that optimize plant performance in response to environmental challenges. The best-known mitochondrial retrograde signaling pathway involves stress-induced activation of the transcription factor NAC DOMAIN CONTAINING PROTEIN 17 (ANAC017), which initiates protective responses to stress-induced mitochondrial dysfunction in Arabidopsis (Arabidopsis thaliana). Posttranslational control of the elicited responses, however, remains poorly understood.

Evolutionary conservation and post-translational control of S-adenosyl-L-homocysteine hydrolase in land plants.

Trans-methylation reactions are intrinsic to cellular metabolism in all living organisms. In land plants, a range of substrate-specific methyltransferases catalyze the methylation of DNA, RNA, proteins, cell wall components and numerous species-specific metabolites, thereby providing means for growth and acclimation in various terrestrial habitats. Trans-methylation reactions consume vast amounts of S-adenosyl-L-methionine (SAM) as a methyl donor in several cellular compartments.

Global proteome response of Synechocystis 6803 to extreme copper environments applied to control the activity of the inducible petJ promoter.

Aims: Cyanobacteria are prokaryotes performing oxygenic photosynthesis, and they can be engineered to harness solar energy for production of commodity and high-value chemicals by means of synthetic biology. The Cu -regulated petJ promoter (P ), which controls the expression of the endogenous cytochrome c553, can be used for expression of foreign products in Synechocystis 6803. We aimed to disclose potential bottlenecks in application of the P in synthetic biology approaches.

Interplay of SpkG kinase and the Slr0151 protein in the phosphorylation of ferredoxin 5 in Synechocystis sp. strain PCC 6803.

In Synechocystis 6803, the ferredoxin 5 (Fd5) phosphoprotein and the S/T protein kinase SpkG are encoded by the slr0148 and slr0152 genes, respectively, which belong to the slr0144-slr0152 cluster. Using a targeted proteomic approach, we showed that SpkG is responsible for the phosphorylation of Fd5 on residues T18 and T72. Sequence alignments and Fd5 structure modelling suggest that these phosphorylation events modulate protein-protein interaction.

Study of O-Phosphorylation Sites in Proteins Involved in Photosynthesis-Related Processes in Synechocystis sp. Strain PCC 6803: Application of the SRM Approach.

O-Phosphorylation has been shown in photosynthesis-related proteins in a cyanobacterium Synechocystis sp. strain PCC 6803 (thereafter Synechocystis 6803), suggesting that phosphorylation of S, T, and Y residues might be important in photosynthesis-related processes. Investigation of biological roles of these phosphorylation events requires confident knowledge of the phosphorylated sites and prospects for their individual assessment.