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  1. Article ; Online: Two-component regulatory systems: The moment of truth.

    Méjean, Vincent

    Research in microbiology

    2016  Volume 167, Issue 1, Page(s) 1–3

    MeSH term(s) Anti-Bacterial Agents/pharmacology ; Bacteria/drug effects ; Bacteria/metabolism ; Bacterial Proteins/antagonists & inhibitors ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biomedical Research ; Histidine Kinase ; Protein Kinases/metabolism
    Chemical Substances Anti-Bacterial Agents ; Bacterial Proteins ; Protein Kinases (EC 2.7.-) ; Histidine Kinase (EC 2.7.13.1)
    Language English
    Publishing date 2016-01
    Publishing country France
    Document type Editorial
    ZDB-ID 1004220-9
    ISSN 1769-7123 ; 0923-2508
    ISSN (online) 1769-7123
    ISSN 0923-2508
    DOI 10.1016/j.resmic.2015.09.004
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  2. Article ; Online: The Shewanella genus: ubiquitous organisms sustaining and preserving aquatic ecosystems.

    Lemaire, Olivier N / Méjean, Vincent / Iobbi-Nivol, Chantal

    FEMS microbiology reviews

    2020  Volume 44, Issue 2, Page(s) 155–170

    Abstract: The Gram-negative Shewanella bacterial genus currently includes about 70 species of mostly aquatic γ--proteobacteria, which were isolated around the globe in a multitude of environments such as surface freshwater and the deepest marine trenches. Their ... ...

    Abstract The Gram-negative Shewanella bacterial genus currently includes about 70 species of mostly aquatic γ--proteobacteria, which were isolated around the globe in a multitude of environments such as surface freshwater and the deepest marine trenches. Their survival in such a wide range of ecological niches is due to their impressive physiological and respiratory versatility. Some strains are among the organisms with the highest number of respiratory systems, depending on a complex and rich metabolic network. Implicated in the recycling of organic and inorganic matter, they are important components of organism-rich oxic/anoxic interfaces, but they also belong to the microflora of a broad group of eukaryotes from metazoans to green algae. Examples of long-term biological interactions like mutualism or pathogeny have been described, although molecular determinants of such symbioses are still poorly understood. Some of these bacteria are key organisms for various biotechnological applications, especially the bioremediation of hydrocarbons and metallic pollutants. The natural ability of these prokaryotes to thrive and detoxify deleterious compounds explains their use in wastewater treatment, their use in energy generation by microbial fuel cells and their importance for resilience of aquatic ecosystems.
    MeSH term(s) Aquatic Organisms/physiology ; Ecosystem ; Environmental Microbiology ; Industrial Microbiology ; Shewanella/classification ; Shewanella/physiology ; Symbiosis
    Language English
    Publishing date 2020-01-22
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 283740-7
    ISSN 1574-6976 ; 0168-6445
    ISSN (online) 1574-6976
    ISSN 0168-6445
    DOI 10.1093/femsre/fuz031
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  3. Article ; Online: Combining two optimized and affordable methods to assign chemoreceptors to a specific signal.

    Boyeldieu, Anne / Ali Chaouche, Amine / Méjean, Vincent / Jourlin-Castelli, Cécile

    Analytical biochemistry

    2021  Volume 620, Page(s) 114139

    Abstract: Chemotaxis allows bacteria to detect specific compounds and move accordingly. This pathway involves signal detection by chemoreceptors (MCPs). Attributing a chemoreceptor to a ligand is difficult because there is a lot of redundancy in the MCPs that ... ...

    Abstract Chemotaxis allows bacteria to detect specific compounds and move accordingly. This pathway involves signal detection by chemoreceptors (MCPs). Attributing a chemoreceptor to a ligand is difficult because there is a lot of redundancy in the MCPs that recognize a single ligand. We propose a methodology to define which chemoreceptors bind a given ligand. First, an MCP is overproduced to increase sensitivity to the ligand(s) it recognizes, thus promoting accumulation of cells around an agarose plug containing a low attractant concentration. Second, the ligand-binding domain (LBD) of the chemoreceptor is fused to maltose-binding protein (MBP), which facilitates purification and provides a control for a thermal shift assay (TSA). An increase in the melting temperature of the LBD in the presence of the ligand indicates that the chemoreceptor directly binds it. We showed that overexpression of two Shewanella oneidensis chemoreceptors (SO_0987 and SO_1056) promoted swimming toward an agarose plug containing a low concentration of chromate. The LBD of each of the two chemoreceptors was fused to MBP. A TSA revealed that only the LBD from SO_1056 had its melting temperature increased by chromate. In conclusion, we describe an efficient approach to define chemoreceptor-ligand pairs before undertaking more-sophisticated biochemical and structural studies.
    MeSH term(s) Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Ligands ; Maltose-Binding Proteins/chemistry ; Shewanella/chemistry ; Transition Temperature
    Chemical Substances Bacterial Proteins ; Ligands ; Maltose-Binding Proteins
    Language English
    Publishing date 2021-02-20
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1110-1
    ISSN 1096-0309 ; 0003-2697
    ISSN (online) 1096-0309
    ISSN 0003-2697
    DOI 10.1016/j.ab.2021.114139
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  4. Article: The Tol-Pal system of Escherichia coli plays an unexpected role in the import of the oxyanions chromate and phosphate

    Chaouche, Amine Ali / Houot, Laetitia / Duché, Denis / Iobbi-Nivol, Chantal / Giudici-Orticoni, Marie-Thérèse / Fons, Michel / Méjean, Vincent

    Research in microbiology. 2022 May 24,

    2022  

    Abstract: Chromate is a toxic metal that enters bacteria by using oxyanion importers. Here, we show that each mutant of the Tol-Pal system of Escherichia coli exhibited increased chromate resistance. This system, which spans the cell envelope, plays a major role ... ...

    Abstract Chromate is a toxic metal that enters bacteria by using oxyanion importers. Here, we show that each mutant of the Tol-Pal system of Escherichia coli exhibited increased chromate resistance. This system, which spans the cell envelope, plays a major role in envelope integrity and septation. The ΔtolQR mutant accumulated three-fold less chromate than the wild-type. Addition of phosphate but not sulfate to rich medium drastically reduced chromate toxicity and import in the wild-type strain. Furthermore, the intracellular concentration of free inorganic phosphate was significantly reduced for the ΔtolR mutant in comparison to the wild-type strain. Moreover, extracellular labelled phosphate was significantly less incorporated into the ΔtolR mutant. Finally, two distinct TolQR mutant complexes, specifically affected in Tol-Pal energization without affecting the TolQRA complex structure, did not complement the ΔtolQR mutant for inorganic phosphate accumulation. We thus propose that, while the Pst system is well known to import inorganic phosphate, the Tol-Pal system participates to phosphate uptake in particular at medium to high extracellular phosphate concentrations. Since mutations disabling the Tol-Pal system lead to pleiotropic effects, chromate resistance and reduced inorganic phosphate import could occur from an indirect effect of mutations in components of the Tol-Pal system.
    Keywords Escherichia coli ; chromates ; imports ; mutants ; oxyanions ; phosphates ; research ; sulfates ; toxicity
    Language English
    Dates of publication 2022-0524
    Publishing place Elsevier Masson SAS
    Document type Article
    Note Pre-press version
    ZDB-ID 1004220-9
    ISSN 1769-7123 ; 0923-2508
    ISSN (online) 1769-7123
    ISSN 0923-2508
    DOI 10.1016/j.resmic.2022.103967
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  5. Article: Combining two optimized and affordable methods to assign chemoreceptors to a specific signal

    Boyeldieu, Anne / Ali Chaouche, Amine / Méjean, Vincent / Jourlin-Castelli, Cécile

    Analytical biochemistry. 2021 May 01, v. 620

    2021  

    Abstract: Chemotaxis allows bacteria to detect specific compounds and move accordingly. This pathway involves signal detection by chemoreceptors (MCPs). Attributing a chemoreceptor to a ligand is difficult because there is a lot of redundancy in the MCPs that ... ...

    Abstract Chemotaxis allows bacteria to detect specific compounds and move accordingly. This pathway involves signal detection by chemoreceptors (MCPs). Attributing a chemoreceptor to a ligand is difficult because there is a lot of redundancy in the MCPs that recognize a single ligand. We propose a methodology to define which chemoreceptors bind a given ligand. First, an MCP is overproduced to increase sensitivity to the ligand(s) it recognizes, thus promoting accumulation of cells around an agarose plug containing a low attractant concentration. Second, the ligand-binding domain (LBD) of the chemoreceptor is fused to maltose-binding protein (MBP), which facilitates purification and provides a control for a thermal shift assay (TSA). An increase in the melting temperature of the LBD in the presence of the ligand indicates that the chemoreceptor directly binds it. We showed that overexpression of two Shewanella oneidensis chemoreceptors (SO_0987 and SO_1056) promoted swimming toward an agarose plug containing a low concentration of chromate. The LBD of each of the two chemoreceptors was fused to MBP. A TSA revealed that only the LBD from SO_1056 had its melting temperature increased by chromate. In conclusion, we describe an efficient approach to define chemoreceptor-ligand pairs before undertaking more-sophisticated biochemical and structural studies.
    Keywords Shewanella oneidensis ; agarose ; chemoreceptors ; chemotaxis ; chromates ; ligands ; temperature
    Language English
    Dates of publication 2021-0501
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1110-1
    ISSN 1096-0309 ; 0003-2697
    ISSN (online) 1096-0309
    ISSN 0003-2697
    DOI 10.1016/j.ab.2021.114139
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  6. Article ; Online: The Tol-Pal system of Escherichia coli plays an unexpected role in the import of the oxyanions chromate and phosphate.

    Ali Chaouche, Amine / Houot, Laetitia / Duché, Denis / Iobbi-Nivol, Chantal / Giudici-Orticoni, Marie-Thérèse / Fons, Michel / Méjean, Vincent

    Research in microbiology

    2022  Volume 173, Issue 8, Page(s) 103967

    Abstract: Chromate is a toxic metal that enters bacteria by using oxyanion importers. Here, we show that each mutant of the Tol-Pal system of Escherichia coli exhibited increased chromate resistance. This system, which spans the cell envelope, plays a major role ... ...

    Abstract Chromate is a toxic metal that enters bacteria by using oxyanion importers. Here, we show that each mutant of the Tol-Pal system of Escherichia coli exhibited increased chromate resistance. This system, which spans the cell envelope, plays a major role in envelope integrity and septation. The ΔtolQR mutant accumulated three-fold less chromate than the wild-type. Addition of phosphate but not sulfate to rich medium drastically reduced chromate toxicity and import in the wild-type strain. Furthermore, the intracellular concentration of free inorganic phosphate was significantly reduced for the ΔtolR mutant in comparison to the wild-type strain. Moreover, extracellular labeled phosphate was significantly less incorporated into the ΔtolR mutant. Finally, two distinct TolQR mutant complexes, specifically affected in Tol-Pal energization without affecting the TolQRA complex structure, did not complement the ΔtolQR mutant for inorganic phosphate accumulation. We thus propose that, while the Pst system is well known to import inorganic phosphate, the Tol-Pal system participates to phosphate uptake in particular at medium to high extracellular phosphate concentrations. Since mutations disabling the Tol-Pal system lead to pleiotropic effects, chromate resistance and reduced inorganic phosphate import could occur from an indirect effect of mutations in components of the Tol-Pal system.
    MeSH term(s) Escherichia coli/genetics ; Escherichia coli Proteins/genetics ; Chromates ; Phosphates
    Chemical Substances Escherichia coli Proteins ; Chromates ; Phosphates
    Language English
    Publishing date 2022-06-01
    Publishing country France
    Document type Journal Article
    ZDB-ID 1004220-9
    ISSN 1769-7123 ; 0923-2508
    ISSN (online) 1769-7123
    ISSN 0923-2508
    DOI 10.1016/j.resmic.2022.103967
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  7. Article ; Online: Multiple detection of both attractants and repellents by the dCache-chemoreceptor SO_1056 of Shewanella oneidensis.

    Boyeldieu, Anne / Poli, Jean-Pierre / Ali Chaouche, Amine / Fierobe, Henri-Pierre / Giudici-Orticoni, Marie-Thérèse / Méjean, Vincent / Jourlin-Castelli, Cécile

    The FEBS journal

    2022  Volume 289, Issue 21, Page(s) 6752–6766

    Abstract: Chemoreceptors are usually transmembrane proteins dedicated to the detection of compound gradients or signals in the surroundings of a bacterium. After detection, they modulate the activation of CheA-CheY, the core of the chemotactic pathway, to allow ... ...

    Abstract Chemoreceptors are usually transmembrane proteins dedicated to the detection of compound gradients or signals in the surroundings of a bacterium. After detection, they modulate the activation of CheA-CheY, the core of the chemotactic pathway, to allow cells to move upwards or downwards depending on whether the signal is an attractant or a repellent, respectively. Environmental bacteria such as Shewanella oneidensis harbour dozens of chemoreceptors or MCPs (methyl-accepting chemotaxis proteins). A recent study revealed that MCP SO_1056 of S. oneidensis binds chromate. Here, we show that this MCP also detects an additional attractant (l-malate) and two repellents (nickel and cobalt). The experiments were performed in vivo by the agarose-in-plug technique after overproducing MCP SO_1056 and in vitro, when possible, by submitting the purified ligand-binding domain (LBD) of SO_1056 to a thermal shift assay (TSA) coupled to isothermal titration calorimetry (ITC). ITC assays revealed a K
    MeSH term(s) Malates ; Chemotaxis ; Nickel ; Bacterial Proteins/metabolism ; Methyl-Accepting Chemotaxis Proteins
    Chemical Substances malic acid (817L1N4CKP) ; Malates ; Nickel (7OV03QG267) ; Bacterial Proteins ; Methyl-Accepting Chemotaxis Proteins
    Language English
    Publishing date 2022-06-24
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.16548
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  8. Article ; Online: Multiple detection of both attractants and repellents by the dCache‐chemoreceptor SO_1056 of Shewanella oneidensis

    Boyeldieu, Anne / Poli, Jean‐Pierre / Ali Chaouche, Amine / Fierobe, Henri‐Pierre / Giudici‐Orticoni, Marie‐Thérèse / Méjean, Vincent / Jourlin‐Castelli, Cécile

    The FEBS Journal. 2022 Nov., v. 289, no. 21 p.6752-6766

    2022  

    Abstract: Chemoreceptors are usually transmembrane proteins dedicated to the detection of compound gradients or signals in the surroundings of a bacterium. After detection, they modulate the activation of CheA‐CheY, the core of the chemotactic pathway, to allow ... ...

    Abstract Chemoreceptors are usually transmembrane proteins dedicated to the detection of compound gradients or signals in the surroundings of a bacterium. After detection, they modulate the activation of CheA‐CheY, the core of the chemotactic pathway, to allow cells to move upwards or downwards depending on whether the signal is an attractant or a repellent, respectively. Environmental bacteria such as Shewanella oneidensis harbour dozens of chemoreceptors or MCPs (methyl‐accepting chemotaxis proteins). A recent study revealed that MCP SO_1056 of S. oneidensis binds chromate. Here, we show that this MCP also detects an additional attractant (l‐malate) and two repellents (nickel and cobalt). The experiments were performed in vivo by the agarose‐in‐plug technique after overproducing MCP SO_1056 and in vitro, when possible, by submitting the purified ligand‐binding domain (LBD) of SO_1056 to a thermal shift assay (TSA) coupled to isothermal titration calorimetry (ITC). ITC assays revealed a KD of 3.4 μm for l‐malate and of 47.7 μm for nickel. We conclude that MCP SO_1056 binds attractants and repellents of unrelated composition. The LBD of SO_1056 belongs to the double Cache_1 family and is highly homologous to PctA, a chemoreceptor from Pseudomonas aeruginosa that detects several amino acids. Therefore, LBDs of the same family can bind diverse compounds, confirming that experimental approaches are required to define accurate LBD‐binding molecules or signals.
    Keywords Pseudomonas aeruginosa ; Shewanella oneidensis ; attractants ; bacteria ; calorimetry ; chemoreceptors ; chemotaxis ; chromates ; cobalt ; nickel ; titration
    Language English
    Dates of publication 2022-11
    Size p. 6752-6766.
    Publishing place John Wiley & Sons, Ltd
    Document type Article ; Online
    Note JOURNAL ARTICLE
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.16548
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  9. Article ; Online: Interplay between the Hsp90 Chaperone and the HslVU Protease To Regulate the Level of an Essential Protein in Shewanella oneidensis.

    Honoré, Flora Ambre / Maillot, Nathanael Jean / Méjean, Vincent / Genest, Olivier

    mBio

    2019  Volume 10, Issue 3

    Abstract: Protein synthesis, folding, and degradation are an accurately regulated process occurring in every organism and called proteostasis. This process is essential to maintain a healthy proteome since proteostasis dysregulation is responsible for devastating ... ...

    Abstract Protein synthesis, folding, and degradation are an accurately regulated process occurring in every organism and called proteostasis. This process is essential to maintain a healthy proteome since proteostasis dysregulation is responsible for devastating cellular issues. Proteostasis is controlled by a complex network of molecular chaperones and proteases. Among them, eukaryotic Hsp90, assisted by many cochaperones and the Hsp70 chaperone system, plays a major role in activating hundreds of client proteins, and Hsp90 inhibition usually leads to proteasomal degradation of these clients. In bacteria, however, the precise function of Hsp90 remains quite unclear, and only a few clients are known. Recently, we have shown that Hsp90 is essential at elevated temperature in the aquatic model bacterium
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Endopeptidase Clp/genetics ; Endopeptidase Clp/metabolism ; Gene Expression Regulation, Bacterial ; HSP70 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/metabolism ; HSP90 Heat-Shock Proteins/genetics ; HSP90 Heat-Shock Proteins/metabolism ; Protein Binding ; Protein Folding ; Proteome ; Proteostasis/genetics ; Shewanella/enzymology ; Shewanella/genetics
    Chemical Substances Bacterial Proteins ; HSP70 Heat-Shock Proteins ; HSP90 Heat-Shock Proteins ; Proteome ; Endopeptidase Clp (EC 3.4.21.92)
    Language English
    Publishing date 2019-05-14
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mBio.00269-19
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  10. Article ; Online: The regulation of Moco biosynthesis and molybdoenzyme gene expression by molybdenum and iron in bacteria.

    Zupok, Arkadiusz / Iobbi-Nivol, Chantal / Méjean, Vincent / Leimkühler, Silke

    Metallomics : integrated biometal science

    2019  Volume 11, Issue 10, Page(s) 1602–1624

    Abstract: Bacterial molybdoenzymes are key enzymes involved in the global sulphur, nitrogen and carbon cycles. These enzymes require the insertion of the molybdenum cofactor (Moco) into their active sites and are able to catalyse a large range of redox-reactions. ... ...

    Abstract Bacterial molybdoenzymes are key enzymes involved in the global sulphur, nitrogen and carbon cycles. These enzymes require the insertion of the molybdenum cofactor (Moco) into their active sites and are able to catalyse a large range of redox-reactions. Escherichia coli harbours nineteen different molybdoenzymes that require a tight regulation of their synthesis according to substrate availability, oxygen availability and the cellular concentration of molybdenum and iron. The synthesis and assembly of active molybdoenzymes are regulated at the level of transcription of the structural genes and of translation in addition to the genes involved in Moco biosynthesis. The action of global transcriptional regulators like FNR, NarXL/QP, Fur and ArcA and their roles on the expression of these genes is described in detail. In this review we focus on what is known about the molybdenum- and iron-dependent regulation of molybdoenzyme and Moco biosynthesis genes in the model organism E. coli. The gene regulation in E. coli is compared to two other well studied model organisms Rhodobacter capsulatus and Shewanella oneidensis.
    MeSH term(s) Bacteria/genetics ; Bacteria/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biosynthetic Pathways ; Coenzymes/genetics ; Coenzymes/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Iron/metabolism ; Metalloproteins/genetics ; Metalloproteins/metabolism ; Molybdenum/metabolism ; Multigene Family ; Pteridines/metabolism ; Rhodobacter capsulatus/genetics ; Rhodobacter capsulatus/metabolism ; Shewanella/genetics ; Shewanella/metabolism
    Chemical Substances Bacterial Proteins ; Coenzymes ; Metalloproteins ; Pteridines ; Molybdenum (81AH48963U) ; molybdenum cofactor (ATN6EG42UQ) ; Iron (E1UOL152H7)
    Language English
    Publishing date 2019-09-04
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2474317-3
    ISSN 1756-591X ; 1756-5901
    ISSN (online) 1756-591X
    ISSN 1756-5901
    DOI 10.1039/c9mt00186g
    Database MEDical Literature Analysis and Retrieval System OnLINE

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