ArticleJournal of bacteriology2013
The Synechocystis PCC6803 MerA-like enzyme operates in the reduction of both mercury and uranium under the control of the glutaredoxin 1 enzyme.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 46 citations in OpenAlex.
- The Glutathione System: A Journey from Cyanobacteria to Higher Eukaryotes.Antioxidants (Basel, Switzerland) · 2023Review
- 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
- Expanded Diversity and Phylogeny ofFrontiers in microbiology · 2021Article
- Recent Advances in the Photoautotrophic Metabolism of Cyanobacteria: Biotechnological Implications.Life (Basel, Switzerland) · 2020Review
- A Comparison of Constitutive and Inducible Non-Endogenous Keto-Carotenoids Biosynthesis inMicroorganisms · 2019Article
- A putative merR family transcription factor Slr0701 regulates mercury inducible expression of MerA in the cyanobacterium Synechocystis sp. PCC6803.MicrobiologyOpen · 2019Article
- Article
- FirstFrontiers in microbiology · 2019Article
- From Cyanobacteria to Human, MAPEG-Type Glutathione-S-Transferases Operate in Cell Tolerance to Heat, Cold, and Lipid Peroxidation.Frontiers in microbiology · 2019Article
- Comparative Genomics of DNA Recombination and Repair in Cyanobacteria: Biotechnological Implications.Frontiers in microbiology · 2016Review
- Microbial DNA records historical delivery of anthropogenic mercury.The ISME journal · 2015Article
- Redox regulation by reversible protein S-thiolation in bacteria.Frontiers in microbiology · 2015Review
- Responses to oxidative and heavy metal stresses in cyanobacteria: recent advances.International journal of molecular sciences · 2014Review
- Function and Regulation of Ferredoxins in the Cyanobacterium, Synechocystis PCC6803: Recent Advances.Life (Basel, Switzerland) · 2014Review
- Advances in the function and regulation of hydrogenase in the cyanobacterium Synechocystis PCC6803.International journal of molecular sciences · 2014Review
- Engineering Synechocystis PCC6803 for hydrogen production: influence on the tolerance to oxidative and sugar stresses.PloS one · 2014Article
- Protein Network Signatures Associated with Exogenous Biofuels Treatments in Cyanobacterium Synechocystis sp. PCC 6803.Frontiers in bioengineering and biotechnology · 2014Article
- Glutaredoxins are essential for stress adaptation in the cyanobacterium Synechocystis sp. PCC 6803.Frontiers in plant science · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In a continuing effort to analyze the selectivity/redundancy of the three glutaredoxin (Grx) enzymes of the model cyanobacterium Synechocystis PCC6803, we have characterized an enzyme system that plays a crucial role in protection against two toxic metal pollutants, mercury and uranium. The present data show that Grx1 (Slr1562 in CyanoBase) selectively interacts with the presumptive mercuric reductase protein (Slr1849). This MerA enzyme plays a crucial role in cell defense against both mercuric and uranyl ions, in catalyzing their NADPH-driven reduction. Like MerA, Grx1 operates in cell protection against both mercury and uranium. The Grx1-MerA interaction requires cysteine 86 (C86) of Grx1 and C78 of MerA, which is critical for its reductase activity. MerA can be inhibited by glutathionylation and subsequently reactivated by Grx1, likely through deglutathionylation. The two Grx1 residues C31, which belongs to the redox active site (CX(2)C), and C86, which operates in MerA interactions, are both required for reactivation of MerA. These novel findings emphasize the role of glutaredoxins in tolerance to metal stress as well as the evolutionary conservation of the glutathionylation process, so far described mostly for eukaryotes.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.