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13 results on '"Brugiere, Sabine"'

1. AtVPS13M1 is involved in lipid remodeling in low phosphate and is located at the mitochondria surface in plants

Author

Leterme, Sebastien, primary, Albrieux, Catherine, additional, Brugiere, Sabine, additional, Coute, Yohann, additional, Dellinger, Julien, additional, Gillet, Benjamin, additional, Hughes, Sandrine, additional, Castets, Julie, additional, Bernard, Amelie, additional, Scheuring, David, additional, Schilling, Marion, additional, Jouhet, Juliette, additional, and Michaud, Morgane, additional

Published
2024
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2. A Soluble Metabolon Synthesizes the Isoprenoid Lipid Ubiquinone

Author

Hajj Chehade, Mahmoud, Pelosi, Ludovic, Fyfe, Cameron David, Loiseau, Laurent, Rascalou, Bérengère, Brugière, Sabine, Kazemzadeh, Katayoun, Vo, Chau-Duy-Tam, Ciccone, Lidia, Aussel, Laurent, Couté, Yohann, Fontecave, Marc, Barras, Frédéric, Lombard, Murielle, and Pierrel, Fabien

Published
2019
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3. Argonaute Autoantibodies as Biomarkers in Autoimmune Neurologic Diseases

Author

Do, Le-Duy, Moritz, Christian P., Muñiz-Castrillo, Sergio, Pinto, Anne-Laurie, Tholance, Yannick, Brugiere, Sabine, Couté, Yohann, Stoevesandt, Oda, Taussig, Michael J., Rogemond, Véronique, Vogrig, Alberto, Joubert, Bastien, Ferraud, Karine, Camdessanché, Jean-Philippe, Antoine, Jean-Christophe, and Honnorat, Jérôme

Published
2021
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4. Short- and long-term efficacy of electroconvulsive stimulation in animal models of depression: The essential role of neuronal survival

Author

Jonckheere, Julie, Deloulme, Jean-Christophe, Dall’Igna, Gaëlle, Chauliac, Nicolas, Pelluet, Albane, Nguon, Anne-Sophie, Lentini, Celia, Brocard, Jacques, Denarier, Eric, Brugière, Sabine, Couté, Yohann, Heinrich, Christophe, Porcher, Christophe, Holtzmann, Jérôme, Andrieux, Annie, Suaud-Chagny, Marie-Françoise, and Gory-Fauré, Sylvie

Published
2018
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5. An algal photoenzyme converts fatty acids to hydrocarbons

Author

Sorigué, Damien, Légeret, Bertrand, Cuiné, Stéphan, Blangy, Stéphanie, Moulin, Solène, Billon, Emmanuelle, Richaud, Pierre, Brugière, Sabine, Couté, Yohann, Nurizzo, Didier, Müller, Pavel, Brettel, Klaus, Pignol, David, Arnoux, Pascal, Li-Beisson, Yonghua, Peltier, Gilles, and Beisson, Fred

Published
2017

9. A versatile method for deciphering plant membrane proteomes

Author

Rolland, Norbert, Ferro, Myriam, Ephritikhine, Geneviève, Marmagne, Anne, Ramus, Claire, Brugière, Sabine, Salvi, Daniel, Seigneurin-Berny, Daphné, Bourguignon, Jacques, Barbier-Brygoo, Hélène, Joyard, Jacques, and Garin, Jérome

Published
2006

11. Mixotrophic growth of the extremophile Galdieria sulphuraria reveals the flexibility of its carbon assimilation metabolism

Author

Curien, Gilles, Lyska, Dagmar, Guglielmino, Erika, Westhoff, Phillip, Janetzko, Janina, Tardif, Marianne, Hallopeau, Clement, Brugiere, Sabine, Dal Bo, Davide, Decelle, Johan, Gallet, Benoit, Falconet, Denis, Carone, Michele, Remacle, Claire, Ferro, Myriam, Weber, Andreas P. M., Finazzi, Giovanni, Curien, Gilles, Lyska, Dagmar, Guglielmino, Erika, Westhoff, Phillip, Janetzko, Janina, Tardif, Marianne, Hallopeau, Clement, Brugiere, Sabine, Dal Bo, Davide, Decelle, Johan, Gallet, Benoit, Falconet, Denis, Carone, Michele, Remacle, Claire, Ferro, Myriam, Weber, Andreas P. M., and Finazzi, Giovanni

Abstract

Galdieria sulphuraria is a cosmopolitan microalga found in volcanic hot springs and calderas. It grows at low pH in photoautotrophic (use of light as a source of energy) or heterotrophic (respiration as a source of energy) conditions, using an unusually broad range of organic carbon sources. Previous data suggested that G. sulphuraria cannot grow mixotrophically (simultaneously exploiting light and organic carbon as energy sources), its photosynthetic machinery being repressed by organic carbon. Here, we show that G. sulphuraria SAG21.92 thrives in photoautotrophy, heterotrophy and mixotrophy. By comparing growth, biomass production, photosynthetic and respiratory performances in these three trophic modes, we show that addition of organic carbon to cultures (mixotrophy) relieves inorganic carbon limitation of photosynthesis thanks to increased CO2 supply through respiration. This synergistic effect is lost when inorganic carbon limitation is artificially overcome by saturating photosynthesis with added external CO2. Proteomic and metabolic profiling corroborates this conclusion suggesting that mixotrophy is an opportunistic mechanism to increase intracellular CO2 concentration under physiological conditions, boosting photosynthesis by enhancing the carboxylation activity of Ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco) and decreasing photorespiration. We discuss possible implications of these findings for the ecological success of Galdieria in extreme environments and for biotechnological applications.

Published
2021

13. Human ribosomes from cells with reduced dyskerin levels are intrinsically altered in translation

Author

Domenica Carnicelli, Maurizio Brigotti, Lorenzo Montanaro, Marianna Penzo, Laura Rocchi, Carmine Onofrillo, Sabine Brugière, Yohann Couté, Etude de la dynamique des protéomes (EDyP ), Laboratoire de Biologie à Grande Échelle (BGE - UMR S1038), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Alma Mater Studiorum Università di Bologna [Bologna] (UNIBO), Penzo, Marianna, Rocchi, Laura, Brugiere, Sabine, Carnicelli, Domenica, Onofrillo, Carmine, Coute, Yohann, Brigotti, Maurizio, Montanaro, Lorenzo, Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), and Dipartimento di Patologia Sperimentale, Università di Bologna

Subjects
mRNA translation, [SDV]Life Sciences [q-bio], Cell Cycle Proteins, Ribosome, Biochemistry, Pseudouridine, Dyskerin, 03 medical and health sciences, chemistry.chemical_compound, 0302 clinical medicine, MCF-7 Cell, Reticulocyte, Genetic, Ribosomal protein, Cell Line, Tumor, Cell Cycle Protein, Genetics, medicine, Protein biosynthesis, Humans, Pseudouridylation, RNA, Messenger, Molecular Biology, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, Nuclear Protein, 0303 health sciences, Protein Biosynthesi, Cell-Free System, Medicine (all), Nuclear Proteins, Translation (biology), Telomere, Cell biology, medicine.anatomical_structure, chemistry, RNA, Ribosomal, 030220 oncology & carcinogenesis, Protein Biosynthesis, MCF-7 Cells, Ribosomes, Small nuclear RNA, Human, Biotechnology
Abstract

Dyskerin is a pseudouridine (ψ) synthase involved in fundamental cellular processes including uridine modification in rRNA and small nuclear RNA and telomere stabilization. Dyskerin functions are altered in X-linked dyskeratosis congenita (X-DC) and cancer. Dyskerin's role in rRNA pseudouridylation has been suggested to underlie the alterations in mRNA translation described in cells lacking dyskerin function, although relevant direct evidences are currently lacking. Our purpose was to establish definitely whether defective dyskerin function might determine an intrinsic ribosomal defect leading to an altered synthetic activity. Therefore, ribosomes from dyskerin-depleted human cells were purified and 1) added to a controlled reticulocyte cell-free system devoid of ribosomes to study mRNA translation; 2) analyzed for protein contamination and composition by mass spectrometry, 3) analyzed for global pseudouridylation levels. Ribosomes purified from dyskerin-depleted cells showed altered translational fidelity and internal ribosome entry site (IRES)-mediated translation. These ribosomes displayed reduced uridine modification, whereas they were not different in terms of protein contamination or ribosomal protein composition with respect to ribosomes from matched control cells with full dyskerin activity. In conclusion, lack of dyskerin function in human cells induces a defect in rRNA uridine modification, which is sufficient to alter ribosome activity.

Published
2015

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