The Synechocystis PCC6803 MerA-Like Enzyme Operates in the Reduction of Both Mercury and Uranium under the Control of the Glutaredoxin 1 Enzyme

Marteyn, Benoît; Sakr, Samer; Farci, Sandrine; Bedhomme, Mariette; Chardonnet, Solenne; Decottignies, Paulette; Lemaire, Stéphane D.; Cassier‐Chauvat, Corinne; Chauvat, Franck

doi:10.1128/jb.00272-13

Cited by 43 publications

(56 citation statements)

References 38 publications

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“…In our laboratory, we often used the temperature-controlled system that appeared to combine most of these advantageous properties (Dutheil et al, 2012; Marteyn et al, 2013; Ortega-Ramos et al, 2014) and references therein. This system tightly controls gene expression proportionally to growth temperatures i.e., absence of expression at temperature ≤30°C (the standard growth temperature of our favorite cyanobacterium Synechocystis PCC6803); intermediary expression at intermediate temperature 34–37°C; and strong expression at 39°C (where Synechocystis PCC6803 keep growing well).…”

Section: Resultsmentioning

confidence: 99%

“…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%

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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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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

2016

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“…While homologs of the broadly-distributed Tn501-like MerA (Barkay et al, 2003) and the newly discovered Synechocystislike MerA (Marteyn et al, 2013) were detected among cyanobacterial taxa, low levels of homology (e value of~50 for the entire protein sequence) were noted. For example, the presence of only 9 of 16 conserved amino acid residues in the redox active site of MerA and absence of amino acid residues essential for MerA activity (Barkay et al, 2010;Boyd and Barkay, 2012) question the functionality of Tn501-like MerA among Chloroflexi and the Cyanobacteria.…”

Section: Consistent With Prior Observations On the Intolerance Ofmentioning

confidence: 94%

Microbes in mercury-enriched geothermal springs in western North America

Geesey

Barkay

King

2016

Science of The Total Environment

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Because geothermal environments contain mercury (Hg) from natural sources, microorganisms that evolved in these systems have likely adapted to this element. Knowledge of the interactions between microorganisms and Hg in geothermal systems may assist in understanding the long-term evolution of microbial adaptation to Hg with relevance to other environments where Hg is introduced from anthropogenic sources. A number of microbiological studies with supporting geochemistry have been conducted in geothermal systems across western North America. Approximately 1 in 5 study sites include measurements of Hg. Of all prokaryotic taxa reported across sites with microbiological and accompanying physicochemical data, 42% have been detected at sites in which Hg was measured. Genes specifying Hg reduction and detoxification by microorganisms were detected in a number of hot springs across the region. Archaeal-like sequences, representing two crenarchaeal orders and one order each of the Euryarchaeota and Thaumarchaeota, dominated in metagenomes' MerA (the mercuric reductase protein) inventories, while bacterial homologs were mostly found in one deeply sequenced metagenome. MerA homologs were more frequently found in metagenomes of microbial communities in acidic springs than in circumneutral or high pH geothermal systems, possibly reflecting higher bioavailability of Hg under acidic conditions. MerA homologs were found in hot springs prokaryotic isolates affiliated with Bacteria and Archaea taxa. Acidic sites with high Hg concentrations contain more of Archaea than Bacteria taxa, while the reverse appears to be the case in circumneutral and high pH sites with high Hg concentrations. However, MerA was detected in only a small fraction of the Archaea and Bacteria taxa inhabiting sites containing Hg. Nevertheless, the presence of MerA homologs and their distribution patterns in systems, in which Hg has yet to be measured, demonstrates the potential for detoxification by Hg reduction in these geothermal systems, particularly the low pH springs that are dominated by Archaea.

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“…Meanwhile, we are currently analyzing the influence of glutathionylation on the activity of selected proteins, including the mercuric reductase enzyme 28 Table 1: Sequence of the PCR primers used in this study. Supplemental Table 2: Proteins glutathionylated by BioGSSG in Synechocystis sp.…”

Section: ■ Concluding Remarksmentioning

confidence: 99%

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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The Synechocystis PCC6803 MerA-Like Enzyme Operates in the Reduction of Both Mercury and Uranium under the Control of the Glutaredoxin 1 Enzyme

Cited by 43 publications

References 38 publications

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

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

Microbes in mercury-enriched geothermal springs in western North America

First Proteomic Study of S-Glutathionylation in Cyanobacteria

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