Reactive oxygen species (ROS) are formed in photosystem II (PSII) under various types of abiotic and biotic stresses. It is considered that ROS play a role in chloroplast-to-nucleus retrograde signaling, which changes the nuclear gene expression. However, as ROS lifetime and diffusion are restricted due to the high reactivity towards biomolecules (lipids, pigments, and proteins) and the spatial specificity of signal transduction is low, it is not entirely clear how ROS might transduce signal from the chloroplasts to the nucleus. Biomolecule oxidation was formerly connected solely with damage; nevertheless, the evidence appears that oxidatively modified lipids and pigments are be involved in chloroplast-to-nucleus retrograde signaling due to their long diffusion distance. Moreover, oxidatively modified proteins show high spatial specificity; however, their role in signal transduction from chloroplasts to the nucleus has not been proven yet. The review attempts to summarize and evaluate the evidence for the involvement of ROS in oxidative signaling in PSII.

• Klíčová slova
• Chloroplast-to-nucleus retrograde signaling, Lipid peroxidation, Protein oxidation, Reactive oxygen species,
• MeSH
• chloroplasty * metabolismus   MeSH
• fotosystém II (proteinový komplex) * metabolismus   MeSH
• lipidy MeSH
• oxidační stres MeSH
• reaktivní formy kyslíku metabolismus   MeSH
• signální transdukce fyziologie   MeSH
• Publikační typ
• časopisecké články MeSH
• přehledy MeSH
• Názvy látek
• fotosystém II (proteinový komplex) * MeSH
• lipidy MeSH
• reaktivní formy kyslíku MeSH

Microorganisms produce volatile compounds (VCs) with molecular masses of less than 300 Da that promote plant growth and photosynthesis. Recently, we have shown that small VCs of less than 45 Da other than CO2 are major determinants of plant responses to fungal volatile emissions. However, the regulatory mechanisms involved in the plants' responses to small microbial VCs remain unclear. In Arabidopsis thaliana plants exposed to small fungal VCs, growth promotion is accompanied by reduction of the thiol redox of Calvin-Benson cycle (CBC) enzymes and changes in the levels of shikimate and 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway-related compounds. We hypothesized that plants' responses to small microbial VCs involve post-translational modulation of enzymes of the MEP and shikimate pathways via mechanisms involving redox-activated photosynthesis signaling. To test this hypothesis, we compared the responses of wild-type (WT) plants and a cfbp1 mutant defective in a redox-regulated isoform of the CBC enzyme fructose-1,6-bisphosphatase to small VCs emitted by the fungal phytopathogen Alternaria alternata. Fungal VC-promoted growth and photosynthesis, as well as metabolic and proteomic changes, were substantially weaker in cfbp1 plants than in WT plants. In WT plants, but not in cfbp1 plants, small fungal VCs reduced the levels of both transcripts and proteins of the stromal Clp protease system and enhanced those of plastidial chaperonins and co-chaperonins. Consistently, small fungal VCs promoted the accumulation of putative Clp protease clients including MEP and shikimate pathway enzymes. clpr1-2 and clpc1 mutants with disrupted plastidial protein homeostasis responded weakly to small fungal VCs, strongly indicating that plant responses to microbial volatile emissions require a finely regulated plastidial protein quality control system. Our findings provide strong evidence that plant responses to fungal VCs involve chloroplast-to-nucleus retrograde signaling of redox-activated photosynthesis leading to proteostatic regulation of the MEP and shikimate pathways.

• Klíčová slova
• : Clp protease system, MEP pathway, PQC system, chloroplast-to-nucleus retrograde signaling, plant–microbe interaction, proteostatic regulation, redox regulation,
• Publikační typ
• časopisecké články MeSH

Gun4 is a porphyrin-binding protein that activates magnesium chelatase, a multimeric enzyme catalyzing the first committed step in chlorophyll biosynthesis. In plants, GUN4 has been implicated in plastid-to-nucleus retrograde signaling processes that coordinate both photosystem II and photosystem I nuclear gene expression with chloroplast function. In this work we present the functional analysis of Gun4 from the cyanobacterium Synechocystis sp. PCC 6803. Affinity co-purification of the FLAG-tagged Gun4 with the ChlH subunit of the magnesium chelatase confirmed the association of Gun4 with the enzyme in cyanobacteria. Inactivation of the gun4 gene abolished photoautotrophic growth of the resulting gun4 mutant strain that exhibited a decreased activity of magnesium chelatase. Consequently, the cellular content of chlorophyll-binding proteins was highly inadequate, especially that of proteins of photosystem II. Immunoblot analyses, blue native polyacrylamide gel electrophoresis, and radiolabeling of the membrane protein complexes suggested that the availability of the photosystem II antenna protein CP47 is a limiting factor for the photosystem II assembly in the gun4 mutant.

• MeSH
• buněčná membrána metabolismus   MeSH
• chlorofyl chemie   metabolismus   MeSH
• chloroplasty metabolismus   MeSH
• elektronová mikroskopie MeSH
• fenotyp MeSH
• fluorescenční spektrometrie metody   MeSH
• fotosyntetická reakční centra (proteinové komplexy) chemie   fyziologie   MeSH
• fotosyntéza MeSH
• fotosystém II (proteinový komplex) metabolismus   MeSH
• intracelulární signální peptidy a proteiny genetika   metabolismus   fyziologie   MeSH
• lyasy chemie   MeSH
• mutace MeSH
• porfyriny chemie   MeSH
• sinice metabolismus   MeSH
• světlosběrné proteinové komplexy metabolismus   MeSH
• transmisní elektronová mikroskopie MeSH
• transportní proteiny genetika   fyziologie   MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• chlorofyl MeSH
• fotosyntetická reakční centra (proteinové komplexy) MeSH
• fotosystém II (proteinový komplex) MeSH
• intracelulární signální peptidy a proteiny MeSH
• lyasy MeSH
• magnesium chelatase MeSH Prohlížeč
• photosystem II, chlorophyll-binding protein, CP-47 MeSH Prohlížeč
• porfyriny MeSH
• světlosběrné proteinové komplexy MeSH
• transportní proteiny MeSH