ArticleMicrobiologyOpen2015
CopM is a novel copper-binding protein involved in copper resistance in Synechocystis sp. PCC 6803.
Article in MicrobiologyOpen, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 38 citations in OpenAlex.
- Thiol, His-His Motif, and the Battle over Cu(II) in the Relationship of CopM Metallophore and OprC Outer Membrane Protein.Inorganic chemistry · 2025Article
- Genetic and biochemical determinants in potentially toxic metals resistance and plant growth promotion in Rhizobium sp LBMP-C04.World journal of microbiology & biotechnology · 2024Article
- The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery.The Journal of biological chemistry · 2022Article
- A protease-mediated mechanism regulates the cytochromeProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Current knowledge and recent advances in understanding metabolism of the model cyanobacterium Synechocystis sp. PCC 6803.Bioscience reports · 2020Review
- High density cultivation for efficient sesquiterpenoid biosynthesis in Synechocystis sp. PCC 6803.Scientific reports · 2020Article
- Lethality caused by ADP-glucose accumulation is suppressed by salt-induced carbon flux redirection in cyanobacteria.Journal of experimental botany · 2020Article
- Regulatory systems for gene expression control in cyanobacteria.Applied microbiology and biotechnology · 2020Review
- The Scs disulfide reductase system cooperates with the metallochaperone CueP inThe Journal of biological chemistry · 2019Article
- A secreted metal-binding protein protects necrotrophic phytopathogens from reactive oxygen species.Nature communications · 2019Article
- Characterization of TrxC, an Atypical Thioredoxin Exclusively Present in Cyanobacteria.Antioxidants (Basel, Switzerland) · 2018Article
- Biosafety of biotechnologically important microalgae: intrinsic suicide switch implementation in cyanobacterium Synechocystis sp. PCC 6803.Biology open · 2016Article
- Extracellular Proteins: Novel Key Components of Metal Resistance in Cyanobacteria?Frontiers in microbiology · 2016Article
- c-Type Cytochrome Assembly Is a Key Target of Copper Toxicity within the Bacterial Periplasm.mBio · 2015Article
- Metals in cyanobacteria: analysis of the copper, nickel, cobalt and arsenic homeostasis mechanisms.Life (Basel, Switzerland) · 2014Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Copper resistance system in the cyanobacterium Synechocystis sp. PCC 6803 comprises two operons, copMRS and copBAC, which are expressed in response to copper in the media. copBAC codes for a heavy-metal efflux-resistance nodulation and division (HME-RND) system, while copMRS codes for a protein of unknown function, CopM, and a two-component system CopRS, which controls the expression of these two operons. Here, we report that CopM is a periplasmic protein able to bind Cu(I) with high affinity (KD ~3 × 10(-16) ). Mutants lacking copM showed a sensitive copper phenotype similar to mutants affected in copB, but lower than mutants of the two-component system CopRS, suggesting that CopBAC and CopM constitute two independent resistance mechanisms. Moreover, constitutive expression of copM is able to partially suppress the copper sensitivity of the copR mutant strain, pointing out that CopM per se is able to confer copper resistance. Furthermore, constitutive expression of copM was able to reduce total cellular copper content of the copR mutant to the levels determined in the wild-type (WT) strain. Finally, CopM was localized not only in the periplasm but also in the extracellular space, suggesting that CopM can also prevent copper accumulation probably by direct copper binding outside the cell.
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