ArticleJournal of bacteriology2009
The glutathione/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. strain PCC 6803.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 72 citations in OpenAlex.
- Molecular Analysis of Two CC-Type Glutaredoxins from the Model LegumeInternational journal of molecular sciences · 2026Article
- Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with glutathione for protein disulfide reduction.Nature communications · 2024Article
- Whole Genome Sequence Analysis ofMicroorganisms · 2023Article
- The Glutathione System: A Journey from Cyanobacteria to Higher Eukaryotes.Antioxidants (Basel, Switzerland) · 2023Review
- Characterization of Two Highly Arsenic-Resistant Caulobacteraceae Strains ofInternational journal of molecular sciences · 2022Article
- Glutathione Is Involved in the Reduction of Methylarsenate to Generate Antibiotic Methylarsenite in Enterobacter sp. Strain CZ-1.Applied and environmental microbiology · 2022Article
- Spectroscopic and functional characterization of the [2Fe-2S] scaffold protein Nfu from Synechocystis PCC6803.Biochimie · 2022Article
- Assessment ofFrontiers in microbiology · 2022Article
- Comparison of alternative integration sites in the chromosome and the native plasmids of the cyanobacterium Synechocystis sp. PCC 6803 in respect to expression efficiency and copy number.Microbial cell factories · 2021Article
- Genetic, Genomics, and Responses to Stresses in Cyanobacteria: Biotechnological Implications.Genes · 2021Review
- Antioxidant ability of glutaredoxins and their role in symbiotic nitrogen fixation inApplied and environmental microbiology · 2021Article
- Real-time monitoring of the in vivo redox state transition using the ratiometric redox state sensor protein FROG/B.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- ArxA FromFrontiers in microbiology · 2019Article
- Co-expression of Cyanobacterial Genes for Arsenic Methylation and Demethylation inFrontiers in microbiology · 2017Article
- Transcriptomic analysis illuminates genes involved in chlorophyll synthesis after nitrogen starvation in Acaryochloris sp. CCMEE 5410.Photosynthesis research · 2016Article
- Regulatory Activities of Four ArsR Proteins in Agrobacterium tumefaciens 5A.Applied and environmental microbiology · 2016Article
- Probing Synechocystis-Arsenic Interactions through Extracellular Nanowires.Frontiers in microbiology · 2016Article
- A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction.The Journal of biological chemistry · 2015Article
- Responses to oxidative and heavy metal stresses in cyanobacteria: recent advances.International journal of molecular sciences · 2014Review
- Metals in cyanobacteria: analysis of the copper, nickel, cobalt and arsenic homeostasis mechanisms.Life (Basel, Switzerland) · 2014Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arsenic resistance in Synechocystis sp. strain PCC 6803 is mediated by an operon of three genes in which arsC codes for an arsenate reductase with unique characteristics. Here we describe the identification of two additional and nearly identical genes coding for arsenate reductases in Synechocystis sp. strain PCC 6803, which we have designed arsI1 and arsI2, and the biochemical characterization of both ArsC (arsenate reductase) and ArsI. Functional analysis of single, double, and triple mutants shows that both ArsI enzymes are active arsenate reductases but that their roles in arsenate resistance are essential only in the absence of ArsC. Based on its biochemical properties, ArsC belongs to a family that, though related to thioredoxin-dependent arsenate reductases, uses the glutathione/glutaredoxin system for reduction, whereas ArsI belongs to the previously known glutaredoxin-dependent family. We have also analyzed the role in arsenate resistance of the three glutaredoxins present in Synechocystis sp. strain PCC 6803 both in vitro and in vivo. Only the dithiolic glutaredoxins, GrxA (glutaredoxin A) and GrxB (glutaredoxin B), are able to donate electrons to both types of reductases in vitro, while GrxC (glutaredoxin C), a monothiolic glutaredoxin, is unable to donate electrons to either type. Analysis of glutaredoxin mutant strains revealed that only those lacking the grxA gene have impaired arsenic resistance.
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