The activity of the Synechocystis PCC6803 AbrB2 regulator of hydrogen production can be post-translationally controlled through glutathionylation

Sakr, Samer; Dutheil, Jérémy; Saenkham, Panatda; Bottin, Hervé; Leplat, Christophe; Ortega-Ramos, Marcia; Aude, Jean-Christophe; Chapuis, Violaine; Guédeney, Geneviève; Decottignies, Paulette; Lemaire, Stéphane D.; Cassier‐Chauvat, Corinne; Chauvat, Franck

doi:10.1016/j.ijhydene.2013.07.124

Cited by 25 publications

(29 citation statements)

References 34 publications

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“…Proteins were then loaded on non-reducing SDS-PAGE and analyzed by Western blot using anti-biotin antibodies as previously described. 29 In Vitro Glutathionylation of PrxII with GSSG and MALDI-TOF Analysis Recombinant PrxII at a concentration of 20 μM was incubated with 5 mM GSSG dissolved in 100 mM Tris-HCl pH 8.3. Aliquots were withdrawn and analyzed by MALDI-TOF mass spectrometry as previously described.…”

Section: In Vitro Glutathionylation Of Recombinant Proteins Using Biomentioning

confidence: 99%

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First Proteomic Study of S-Glutathionylation in Cyanobacteria

et al. 2014

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Glutathionylation, the reversible post-translational formation of a mixed disulfide between a cysteine residue and glutathione (GSH), is a crucial mechanism for signal transduction and regulation of protein function. Until now this reversible redox modification was studied mainly in eukaryotic cells. Here we report a large-scale proteomic analysis of glutathionylation in a photosynthetic prokaryote, the model cyanobacterium Synechocystis sp. PCC6803. Treatment of acellular extracts with N,N-biotinyl glutathione disulfide (BioGSSG) induced glutathionylation of numerous proteins, which were subsequently isolated by affinity chromatography on streptavidin columns and identified by nano LC-MS/MS analysis. Potential sites of glutathionylation were also determined for 125 proteins following tryptic cleavage, streptavidin-affinity purification, and mass spectrometry analysis. Taken together the two approaches allowed the identification of 383 glutathionylatable proteins that participate in a wide range of cellular processes and metabolic pathways such as carbon and nitrogen metabolisms, cell division, stress responses, and H2 production. In addition, the glutathionylation of two putative targets, namely, peroxiredoxin (Sll1621) involved in oxidative stress tolerance and 3-phosphoglycerate dehydrogenase (Sll1908) acting on amino acids metabolism, was confirmed by biochemical studies on the purified recombinant proteins. These results suggest that glutathionylation constitutes a major mechanism of global regulation of the cyanobacterial metabolism under oxidative stress conditions.

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Section: In Vitro Glutathionylation Of Recombinant Proteins Using Biomentioning

confidence: 99%

“…PCC6803. 28,29 This organism, the best studied unicellular cyanobacterium, harbors a small sequenced and fully annotated genome, 30 which facilitates proteomic approaches. Synechocystis sp.…”

Section: ■ Introductionmentioning

confidence: 99%

First Proteomic Study of S-Glutathionylation in Cyanobacteria

et al. 2014

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“…strain ATCC29133 (also registered as PCC73102) (Huang et al, 2010; Taton et al, 2014). Such RSF1010-derived plasmids proved useful tools for in vivo studies of (i) gene expression (Marraccini et al, 1993; Mermet-Bouvier and Chauvat, 1994; Mazouni et al, 1998; Figge et al, 2000; Mazouni et al, 2003; Huang et al, 2010; Dutheil et al, 2012); (ii) cell division (Mazouni et al, 2004; Marbouty et al, 2009), DNA repair (Domain et al, 2004); (iii) hydrogen production (Dutheil et al, 2012; Sakr et al, 2013; Ortega-Ramos et al, 2014); (iv) insertion sequence (Cassier-Chauvat et al, 1997); and (v) redox metabolism and responses to heavy metals (Poncelet et al, 1998; Marteyn et al, 2009, 2013). …”

Section: Introductionmentioning

confidence: 99%

Comparative Genomics of DNA Recombination and Repair in Cyanobacteria: Biotechnological Implications

2016

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Cyanobacteria are fascinating photosynthetic prokaryotes that are regarded as the ancestors of the plant chloroplast; the purveyors of oxygen and biomass for the food chain; and promising cell factories for an environmentally friendly production of chemicals. In colonizing most waters and soils of our planet, cyanobacteria are inevitably challenged by environmental stresses that generate DNA damages. Furthermore, many strains engineered for biotechnological purposes can use DNA recombination to stop synthesizing the biotechnological product. Hence, it is important to study DNA recombination and repair in cyanobacteria for both basic and applied research. This review reports what is known in a few widely studied model cyanobacteria and what can be inferred by mining the sequenced genomes of morphologically and physiologically diverse strains. We show that cyanobacteria possess many E. coli-like DNA recombination and repair genes, and possibly other genes not yet identified. E. coli-homolog genes are unevenly distributed in cyanobacteria, in agreement with their wide genome diversity. Many genes are extremely well conserved in cyanobacteria (mutMS, radA, recA, recFO, recG, recN, ruvABC, ssb, and uvrABCD), even in small genomes, suggesting that they encode the core DNA repair process. In addition to these core genes, the marine Prochlorococcus and Synechococcus strains harbor recBCD (DNA recombination), umuCD (mutational DNA replication), as well as the key SOS genes lexA (regulation of the SOS system) and sulA (postponing of cell division until completion of DNA reparation). Hence, these strains could possess an E. coli-type SOS system. In contrast, several cyanobacteria endowed with larger genomes lack typical SOS genes. For examples, the two studied Gloeobacter strains lack alkB, lexA, and sulA; and Synechococcus PCC7942 has neither lexA nor recCD. Furthermore, the Synechocystis PCC6803 lexA product does not regulate DNA repair genes. Collectively, these findings indicate that not all cyanobacteria have an E. coli-type SOS system. Also interestingly, several cyanobacteria possess multiple copies of E. coli-like DNA repair genes, such as Acaryochloris marina MBIC11017 (2 alkB, 3 ogt, 7 recA, 3 recD, 2 ssb, 3 umuC, 4 umuD, and 8 xerC), Cyanothece ATCC51142 (2 lexA and 4 ruvC), and Nostoc PCC7120 (2 ssb and 3 xerC).

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“…On the other hand, Sakr et al [39] found a relationship between protein regulators, oxidative stress and hydrogen production in prokaryotic cyanobacterium Synechocystis PCC6803. They reported that AbrB2 (gene encoding a protein regulator of hydrogen production operon) down-regulates hydrogen production and other stress defense genes in the absence of stress.…”

Section: Discussionmentioning

confidence: 99%