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54. Sécurité alimentaire et climat.

Author

Hatté, Christine, Ciais, Philippe, Heulin, Thierry, Nussaume, Laurent, Rolland, Norbert, and Viovy, Nicolas

Published
2022

55. Crystal Structure of the Chloroplastic Oxoene Reductase ceQORH from Arabidopsis thaliana

Author

Mas Y Mas, Sarah, Curien, Gilles, Giustini, Cécile, Rolland, Norbert, Ferrer, Jean-Luc, Cobessi, David, Institut de biologie structurale (IBS - UMR 5075 ), 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)-Centre National de la Recherche Scientifique (CNRS), Physiologie cellulaire et végétale (LPCV), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-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), FRISBI [ANR-10-INSB-05-02], GRAL within Grenoble Partnership for Structural Biology (PSB) [ANR-10-LABX-49-01], FIP-BM30A- ESRF, HTX- EMBL, ANR-10-LABX-0049,GRAL,Grenoble Alliance for Integrated Structural Cell Biology(2010), Institut de biologie structurale (IBS - UMR 5075), 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)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), ANR-10- LABX-49-01,Labex GRAL,Labex GRAL, Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG)

Subjects
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], γ-ketols, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], oxylipins, α, chloroplast envelope quinone oxidoreductase homolog, lcsh:SB1-1110, Plant Science, lcsh:Plant culture, β-unsaturated carbonyls, ComputingMilieux_MISCELLANEOUS, Original Research, X-ray crystallography
Abstract

International audience; Enzymatic and non-enzymatic peroxidation of polyunsaturated fatty acids give rise to accumulation of aldehydes, ketones, and alpha, beta-unsaturated carbonyls of various lengths, known as oxylipins. Oxylipins with alpha, beta-unsaturated carbonyls are reactive electrophile species and are toxic. Cells have evolved several mechanisms to scavenge reactive electrophile oxylipins and decrease their reactivity such as by coupling with glutathione, or by reduction using NAD(P)H-dependent reductases and dehydrogenases of various substrate specificities. Plant cell chloroplasts produce reactive electrophile oxylipins named gamma-ketols downstream of enzymatic lipid peroxidation. The chloroplast envelope quinone oxidoreductase homolog (ceQORH) from Arabidopsis thaliana was previously shown to reduce the reactive double bond of gamma-ketols. In marked difference with its cytosolic homolog alkenal reductase (AtAER) that displays a high activity toward the ketodiene 13-oxo-9(Z), 11(E)-octadecadienoic acid (13-KODE) and the ketotriene 13-oxo-9(Z), 11(E), 15(Z)-octadecatrienoic acid (13-KOTE), ceQORH binds, but does not reduce, 13-KODE and 13-KOTE. Crystal structures of apo-ceQORH and ceQORH bound to 13-KOTE or to NADP(+) and 13-KOTE have been solved showing a large ligand binding site, also observed in the structure of the cytosolic alkenal/one reductase. Positioning of the alpha, beta-unsaturated carbonyl of 13-KOTE in ceQORH-NADP(+)-13-KOTE, far away from the NADP(+) nicotinamide ring, provides a rational for the absence of activity with the ketodienes and ketotrienes. ceQORH is a monomeric enzyme in solution whereas other enzymes from the quinone oxidoreductase family are stable dimers and a structural explanation of this difference is proposed. A possible in vivo role of ketodienes and ketotrienes binding to ceQORH is also discussed.

Published
2017
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56. HMA6 and HMA8 are two chloroplast Cu+-ATPases with different enzymatic properties

Author

Sautron, Emeline, Mayerhofer, Hubert, Giustini, Cécile, Pro, Danièle, Crouzy, Serge, Ravaud, Stéphanie, Pebay-Peyroula, Eva, Rolland, Norbert, Catty, Patrice, Seigneurin-Berny, Daphné, Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075), 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)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-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), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Recherche Agronomique (INRA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075 ), 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)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-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)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), The Commissariat à l’Energie Atomique et aux Energies Alternatives, the Centre National de la Recherche Scientifique, the French National Institute for Agricultural Research, the University of Grenoble, and the GRAL Labex (Grenoble Alliance for Integrated Structural Cell Biology: ANR-10-LABEX-04), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG)

Subjects
Protein Conformation, arabidopsis, chloroplast, copper, PIB-ATPase, plant biochemistry, thylakoids, transporter, Arabidopsis, Saccharomyces cerevisiae, Adenosine Triphosphate, Lactococcus, Chloroplast Proton-Translocating ATPases, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Phosphorylation, Plastocyanin, Adenosine Triphosphatases, Original Paper, Vegetal Biology, Arabidopsis Proteins, food and beverages, Modélisation et simulation, Original Papers, [INFO.INFO-MO]Computer Science [cs]/Modeling and Simulation, Molecular Docking Simulation, Modeling and Simulation, Biologie végétale
Abstract

In Arabidopsis chloroplasts, HMA8, the thylakoid Cu+-ATPase and HMA6, the envelope Cu+-ATPase, have different enzymatic properties. These differences might be related to the electrostatic properties of the Cu+ release cavities of the transporters or the nature of their Cu acceptor., Copper (Cu) plays a key role in the photosynthetic process as cofactor of the plastocyanin (PC), an essential component of the chloroplast photosynthetic electron transfer chain. Encoded by the nuclear genome, PC is translocated in its apo-form into the chloroplast and the lumen of thylakoids where it is processed to its mature form and acquires Cu. In Arabidopsis, Cu delivery into the thylakoids involves two transporters of the PIB-1 ATPases family, heavy metal associated protein 6 (HMA6) located at the chloroplast envelope and HMA8 at the thylakoid membrane. To gain further insight into the way Cu is delivered to PC, we analysed the enzymatic properties of HMA8 and compared them with HMA6 ones using in vitro phosphorylation assays and phenotypic tests in yeast. These experiments reveal that HMA6 and HMA8 display different enzymatic properties: HMA8 has a higher apparent affinity for Cu+ but a slower dephosphorylation kinetics than HMA6. Modelling experiments suggest that these differences could be explained by the electrostatic properties of the Cu+ releasing cavities of the two transporters and/or by the different nature of their cognate Cu+ acceptors (metallochaperone/PC).

Published
2015

60. Plant organelle proteomics: Collaborating for optimal cell function

Author

Agrawal, Ganesh Kumar, Bourguignon, Jacques, Rolland, Norbert, Ephritikhine, Geneviève, Ferro, Myriam, Jaquinod, Michel, Alexiou, Konstantinos G, Chardot, Thierry, Chakraborty, Niranjan, Jolivet, Pascale, Doonan, John H, Rakwal, Randeep, Laboratory for Biotechnology and Biochemistry (RLABB), Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-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 de Biosciences et de Biotechnologies de Grenoble (ex-IRTSV) (BIG), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut des sciences du végétal (ISV), Centre National de la Recherche Scientifique (CNRS), Université Paris Diderot - Paris 7 (UPD7), Laboratoire d'étude de la dynamique des protéomes (LEDyP), Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), John Innes Centre [Norwich], Biotechnology and Biological Sciences Research Council (BBSRC), Institut Jean-Pierre Bourgin (IJPB), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, National Institute of Plant Genome Research, JNU Campus, Health Technology Research Center (HTRC), National Institute of Advanced Industrial Science and Technology (AIST), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-Université Grenoble Alpes (UGA), Laboratoire d'Etude de la Dynamique des Proteomes, and Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
Organelles, Proteomics, Staining and Labeling, organelle, proteome, Arabidopsis, review, Oryza, plant, cell, Cell Fractionation, Zea mays, Mass Spectrometry, animals, Gene Expression Regulation, Plant, Plant Cells, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, mammalia, Biomarkers, Plant Proteins
Abstract

International audience; Organelle proteomics describes the study of proteins present in organelle at a particular instance during the whole period of their life cycle in a cell. Organelles are specialized membrane bound structures within a cell that function by interacting with cytosolic and luminal soluble proteins making the protein composition of each organelle dynamic. Depending on organism, the total number of organelles within a cell varies, indicating their evolution with respect to protein number and function. For example, one of the striking differences between plant and animal cells is the plastids in plants. Organelles have their own proteins, and few organelles like mitochondria and chloroplast have their own genome to synthesize proteins for specific function and also require nuclear-encoded proteins. Enormous work has been performed on animal organelle proteomics. However, plant organelle proteomics has seen limited work mainly due to: (i) inter-plant and inter-tissue complexity, (ii) difficulties in isolation of subcellular compartments, and (iii) their enrichment and purity. Despite these concerns, the field of organelle proteomics is growing in plants, such as Arabidopsis, rice and maize. The available data are beginning to help better understand organelles and their distinct and/or overlapping functions in different plant tissues, organs or cell types, and more importantly, how protein components of organelles behave during development and with surrounding environments. Studies on organelles have provided a few good reviews, but none of them are comprehensive. Here, we present a comprehensive review on plant organelle proteomics starting from the significance of organelle in cells, to organelle isolation, to protein identification and to biology and beyond. To put together such a systematic, in-depth review and to translate acquired knowledge in a proper and adequate form, we join minds to provide discussion and viewpoints on the collaborative nature of organelles in cell, their proper function and evolution. © 2010 Wiley Periodicals, Inc. Mass Spec Rev.

Published
2011

61. La protéomique des plantes

Author

Rolland, Norbert, Kuntz, Marcel, Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-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 de Biosciences et de Biotechnologies de Grenoble (ex-IRTSV) (BIG), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Dattée, Y., Fellous, M., Gallais, A., Joudrier, P., Pelletier, G. and Ricroch, Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-Université Grenoble Alpes (UGA), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
proteomics, plant, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, protein
Published
2011

63. In vivo spectroscopy and NMR metabolite fingerprinting approaches to connect the dynamics of photosynthetic and metabolic phenotypes in resurrection plant Haberlea rhodopensis during desiccation and recovery

Author

Mladenov, Petko, primary, Finazzi, Giovanni, additional, Bligny, Richard, additional, Moyankova, Daniela, additional, Zasheva, Diana, additional, Boisson, Anne-Marie, additional, Brugière, Sabine, additional, Krasteva, Vasilena, additional, Alipieva, Kalina, additional, Simova, Svetlana, additional, Tchorbadjieva, Magdalena, additional, Goltsev, Vasiliy, additional, Ferro, Myriam, additional, Rolland, Norbert, additional, and Djilianov, Dimitar, additional

Published
2015
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64. Ions channels/transporters and chloroplast regulation

Author

Finazzi, Giovanni, primary, Petroutsos, Dimitris, additional, Tomizioli, Martino, additional, Flori, Serena, additional, Sautron, Emeline, additional, Villanova, Valeria, additional, Rolland, Norbert, additional, and Seigneurin-Berny, Daphné, additional

Published
2015
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66. Membrane protein expression in Lactococcus lactis

Author

Frelet-Barrand, Annie, Boutigny, Sylvain, Kunji, Edmund R S, Rolland, Norbert, Laboratoire de physiologie cellulaire végétale ( LPCV ), Université Joseph Fourier - Grenoble 1 ( UJF ) -Institut National de la Recherche Agronomique ( INRA ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ), MRC Mitochondrial Biology Unit, University of Cambridge [UK] ( CAM ), Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-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), University of Cambridge [UK] (CAM), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), and Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
MESH: Gene Expression, MESH : Cloning, Molecular, MESH : Recombinant Proteins, Blotting, Western, Genetic Vectors, Gene Expression, MESH : Blotting, Western, MESH : Electrophoresis, Polyacrylamide Gel, MESH: Nisin, MESH: Recombinant Proteins, MESH: Genetic Vectors, Strep-tag II, MESH : Nisin, Animals, Humans, MESH: Blotting, Western, MESH: Animals, MESH: Cloning, Molecular, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, protocol, Cloning, Molecular, bacteria, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Nisin, membra ne protein, MESH: Gene Expression Regulation, Bacterial, MESH: Humans, MESH : Humans, Membrane Proteins, Gene Expression Regulation, Bacterial, Recombinant Proteins, MESH : Genetic Vectors, Lactococcus lactis, MESH : Gene Expression, MESH: Lactococcus lactis, MESH : Membrane Proteins, protein overproduction, Cell disruptor, Electrophoresis, Polyacrylamide Gel, MESH: Membrane Proteins, MESH : Animals, MESH : Lactococcus lactis, recombinant protein, MESH: Electrophoresis, Polyacrylamide Gel, biotechnology, MESH : Gene Expression Regulation, Bacterial
Abstract

International audience; Membrane proteins play key roles in cellular physiology, and they are important drug targets. Approximately 25% of all genes identified in sequenced genomes are known to encode membrane proteins; however, the majority have no assigned function. Although the resolution of soluble protein structure has entered the high-throughput stage, only 100 high-resolution structures of membrane proteins have been described until now. Lactococcus lactis is a gram-positive lactic bacterium that has been used traditionally in food fermentations, but it is now used widely in biotechnology for large-scale overproduction of heterologously expressed proteins. Various expression vectors based on either constitutive or inducible promoters exist. The nisin-inducible controlled gene expression (NICE) system is the most suitable for recombinant membrane protein expression allowing for fine control of gene expression based on the autoregulation mechanism of the bacteriocin nisin. Recombinant membrane proteins can be produced with affinity tags for efficient detection and purification from crude membrane protein extracts. The purpose of this chapter is to provide a detailed protocol for the expression of membrane proteins and their detection using the Strep-tag II affinity tag in L. lactis.

Published
2010

67. Screening for new proteins targeted to plastid through alternative or ‘noncanonical’ import

Author

Gall, Sophie Le, Moyet, Lucas, Salvi, Daniel, Bardor, Muriel, Ferro, Myriam, Brugière, Sabine, Masselon, Christophe, Lerouge, Patrice, Rolland, Norbert, Laboratoire de Glycobiologie et Matrice Extracellulaire Végétale (Glyco-MEV), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-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), Laboratoire d'étude de la dynamique des protéomes (LEDyP), Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Physiologie cellulaire et végétale (LPCV), Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Centre National de la Recherche Scientifique (CNRS)

Subjects
[SDV.BV.AP]Life Sciences [q-bio]/Vegetal Biology/Plant breeding, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], [SDV.BDD]Life Sciences [q-bio]/Development Biology, ComputingMilieux_MISCELLANEOUS, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], [SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacy
Abstract

International audience

Published
2009

68. Identification de nouvelles protéines utilisant une voie alternative pour leur import dans les plastes

Author

Gall, Sophie Le, Moyet, Lucas, Salvi, Daniel, Bardor, Muriel, Ferro, Myriam, Brugière, Sabine, Masselon, Christophe, Rolland, Norbert, Lerouge, Patrice, Laboratoire de Glycobiologie et Matrice Extracellulaire Végétale (Glyco-MEV), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Physiologie cellulaire et végétale (LPCV), Université Grenoble Alpes (UGA)-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 Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'étude de la dynamique des protéomes (LEDyP), Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire de physiologie cellulaire végétale (LPCV), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
[SDV.BV.AP]Life Sciences [q-bio]/Vegetal Biology/Plant breeding, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], [SDV.BDD]Life Sciences [q-bio]/Development Biology, ComputingMilieux_MISCELLANEOUS, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], [SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacy
Abstract

International audience

Published
2009

69. Glyco-chloroplast – identification of signals controlling the protein trafficking between the sercretory pathway and the chloroplast

Author

Rolland, Norbert, Lerouge, Patrice, Physiologie cellulaire et végétale (LPCV), Université Grenoble Alpes (UGA)-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 Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Glycobiologie et Matrice Extracellulaire Végétale (Glyco-MEV), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU), Laboratoire de physiologie cellulaire végétale (LPCV), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
[SDV.BV.AP]Life Sciences [q-bio]/Vegetal Biology/Plant breeding, [SDV.BIO]Life Sciences [q-bio]/Biotechnology, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], [SDV.BC.IC]Life Sciences [q-bio]/Cellular Biology/Cell Behavior [q-bio.CB], [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC], [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], [SDV.BDD]Life Sciences [q-bio]/Development Biology, ComputingMilieux_MISCELLANEOUS, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM], [SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacy
Abstract

International audience

Published
2009

70. Purification and fractionation of Arabidopsis membranes for proteomic analyses

Author

Marmagne, Anne, Salvi, Daniel, Rolland, Norbert, Ephritikhine, Geneviève, Joyard, Jacques, Barbier-Brygoo, Hélène, Institut des sciences du végétal (ISV), Centre National de la Recherche Scientifique (CNRS), Laboratoire de physiologie cellulaire végétale (LPCV), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Salinas, J. and Sanchez-Serrano, J.J., Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-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)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
fractionation method, experimental protocols, proteomics, Arabidopsis thaliana, two phase partitioning, protein purification, plant, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, chloroplast envelope membrane, membrane purity, plasma membrane, membrane
Published
2006

71. Deciphering Thylakoid Sub-compartments using a Mass Spectrometry-based Approach

Author

Tomizioli, Martino, primary, Lazar, Cosmin, additional, Brugière, Sabine, additional, Burger, Thomas, additional, Salvi, Daniel, additional, Gatto, Laurent, additional, Moyet, Lucas, additional, Breckels, Lisa M., additional, Hesse, Anne-Marie, additional, Lilley, Kathryn S., additional, Seigneurin-Berny, Daphné, additional, Finazzi, Giovanni, additional, Rolland, Norbert, additional, and Ferro, Myriam, additional

Published
2014
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72. Glycerolipids in photosynthesis: Composition, synthesis and trafficking

Author

Boudière, Laurence, primary, Michaud, Morgane, additional, Petroutsos, Dimitris, additional, Rébeillé, Fabrice, additional, Falconet, Denis, additional, Bastien, Olivier, additional, Roy, Sylvaine, additional, Finazzi, Giovanni, additional, Rolland, Norbert, additional, Jouhet, Juliette, additional, Block, Maryse A., additional, and Maréchal, Eric, additional

Published
2014
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74. Complementary biochemical approaches applied to the identification of plastidial calmodulin-binding proteins

Author

Dell'Aglio, Elisa, primary, Giustini, Cécile, additional, Salvi, Daniel, additional, Brugière, Sabine, additional, Delpierre, Faustine, additional, Moyet, Lucas, additional, Baudet, Mathieu, additional, Seigneurin-Berny, Daphné, additional, Matringe, Michel, additional, Ferro, Myriam, additional, Rolland, Norbert, additional, and Curien, Gilles, additional

Published
2013
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75. Structural Insights into the Nucleotide-Binding Domains of the P1B-type ATPases HMA6 and HMA8 from Arabidopsis thaliana.

Author

Mayerhofer, Hubert, Sautron, Emeline, Rolland, Norbert, Catty, Patrice, Seigneurin-Berny, Daphné, Pebay-Peyroula, Eva, and Ravaud, Stéphanie

Subjects
ARABIDOPSIS thaliana, NUCLEOTIDES, CHLOROPLASTS, PHOTOSYNTHESIS, CHARGE exchange, PLASTOCYANIN, EFFECT of copper on plants, ADENOSINE triphosphatase
Abstract

Copper is a crucial ion in cells, but needs to be closely controlled due to its toxic potential and ability to catalyse the formation of radicals. In chloroplasts, an important step for the proper functioning of the photosynthetic electron transfer chain is the delivery of copper to plastocyanin in the thylakoid lumen. The main route for copper transport to the thylakoid lumen is driven by two PIB-type ATPases, Heavy Metal ATPase 6 (HMA6) and HMA8, located in the inner membrane of the chloroplast envelope and in the thylakoid membrane, respectively. Here, the crystal structures of the nucleotide binding domain of HMA6 and HMA8 from Arabidopsis thaliana are reported at 1.5Å and 1.75Å resolution, respectively, providing the first structural information on plants Cu+-ATPases. The structures reveal a compact domain, with two short helices on both sides of a twisted beta-sheet. A double mutant, aiding in the crystallization, provides a new crystal contact, but also avoids an internal clash highlighting the benefits of construct modifications. Finally, the histidine in the HP motif of the isolated domains, unable to bind ATP, shows a side chain conformation distinct from nucleotide bound structures. [ABSTRACT FROM AUTHOR]

Published
2016
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77. Evidence for a protein transported through the secretory pathway en route to the higher plant chloroplast.

Author

Villarejo, Arsenio, Burén, Stefan, Larsson, Susanne, Déjardin, Annabelle, Monné, Magnus, Rudhe, Charlotta, Karlsson, Jan, Jansson, Stefan, Lerouge, Patrice, Rolland, Norbert, von Heijne, Gunnar, Grebe, Markus, Bako, Laszlo, Samuelsson, Göran, Villarejo, Arsenio, Burén, Stefan, Larsson, Susanne, Déjardin, Annabelle, Monné, Magnus, Rudhe, Charlotta, Karlsson, Jan, Jansson, Stefan, Lerouge, Patrice, Rolland, Norbert, von Heijne, Gunnar, Grebe, Markus, Bako, Laszlo, and Samuelsson, Göran

Abstract

In contrast to animal and fungal cells, green plant cells contain one or multiple chloroplasts, the organelle(s) in which photosynthetic reactions take place. Chloroplasts are believed to have originated from an endosymbiotic event and contain DNA that codes for some of their proteins. Most chloroplast proteins are encoded by the nuclear genome and imported with the help of sorting signals that are intrinsic parts of the polypeptides. Here, we show that a chloroplast-located protein in higher plants takes an alternative route through the secretory pathway, and becomes N-glycosylated before entering the chloroplast.

Published
2005
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80. Heterologous Expression of Membrane Proteins: Choosing the Appropriate Host

Author

Bernaudat, Florent, primary, Frelet-Barrand, Annie, additional, Pochon, Nathalie, additional, Dementin, Sébastien, additional, Hivin, Patrick, additional, Boutigny, Sylvain, additional, Rioux, Jean-Baptiste, additional, Salvi, Daniel, additional, Seigneurin-Berny, Daphné, additional, Richaud, Pierre, additional, Joyard, Jacques, additional, Pignol, David, additional, Sabaty, Monique, additional, Desnos, Thierry, additional, Pebay-Peyroula, Eva, additional, Darrouzet, Elisabeth, additional, Vernet, Thierry, additional, and Rolland, Norbert, additional

Published
2011
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83. MASCP Gator: An Aggregation Portal for the Visualization of Arabidopsis Proteomics Data

Author

Joshi, Hiren J., primary, Hirsch-Hoffmann, Matthias, additional, Baerenfaller, Katja, additional, Gruissem, Wilhelm, additional, Baginsky, Sacha, additional, Schmidt, Robert, additional, Schulze, Waltraud X., additional, Sun, Qi, additional, van Wijk, Klaas J., additional, Egelhofer, Volker, additional, Wienkoop, Stefanie, additional, Weckwerth, Wolfram, additional, Bruley, Christophe, additional, Rolland, Norbert, additional, Toyoda, Tetsuro, additional, Nakagami, Hirofumi, additional, Jones, Alexandra M., additional, Briggs, Steven P., additional, Castleden, Ian, additional, Tanz, Sandra K., additional, Millar, A. Harvey, additional, and Heazlewood, Joshua L., additional

Published
2010
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84. Plant organelle proteomics: Collaborating for optimal cell function

Author

Agrawal, Ganesh Kumar, primary, Bourguignon, Jacques, additional, Rolland, Norbert, additional, Ephritikhine, Geneviève, additional, Ferro, Myriam, additional, Jaquinod, Michel, additional, Alexiou, Konstantinos G., additional, Chardot, Thierry, additional, Chakraborty, Niranjan, additional, Jolivet, Pascale, additional, Doonan, John H., additional, and Rakwal, Randeep, additional

Published
2010
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86. Lactococcus lactis, an Alternative System for Functional Expression of Peripheral and Intrinsic Arabidopsis Membrane Proteins

Author

Frelet-Barrand, Annie, primary, Boutigny, Sylvain, additional, Moyet, Lucas, additional, Deniaud, Aurélien, additional, Seigneurin-Berny, Daphné, additional, Salvi, Daniel, additional, Bernaudat, Florent, additional, Richaud, Pierre, additional, Pebay-Peyroula, Eva, additional, Joyard, Jacques, additional, and Rolland, Norbert, additional

Published
2010
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88. Chlamydomonas proteomics

Author

Rolland, Norbert, primary, Atteia, Ariane, additional, Decottignies, Paulette, additional, Garin, Jérôme, additional, Hippler, Michael, additional, Kreimer, Georg, additional, Lemaire, Stéphane D, additional, Mittag, Maria, additional, and Wagner, Volker, additional

Published
2009
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92. HMA6 and HMA8 are two chloroplast Cu + -ATPases with different enzymatic properties.

Author

Sautron, Emeline, Mayerhofer, Hubert, Giustini, Cécile, Pro, Danièle, Crouzy, Serge, Ravaud, Stèphanie, Pebay-Peyroula, Eva, Rolland, Norbert, Catty, Patrice, and Seigneurin-Berny, Daphnè

Subjects
CHLOROPLASTS, ADENOSINE triphosphatase, PHOTOSYNTHESIS, CHARGE exchange, PLASTOCYANIN, ARABIDOPSIS
Abstract

Copper (Cu) plays a key role in the photosynthetic process as cofactor of the plastocyanin (PC), an essential component of the chloroplast photosynthetic electron transfer chain. Encoded by the nuclear genome, PC is translocated in its apo-form into the chloroplast and the lumen of thylakoids where it is processed to its mature form and acquires Cu. In Arabidopsis, Cu delivery into the thylakoids involves two transporters of the PIB-1 ATPases family, heavy metal associated protein 6 (HMA6) located at the chloroplast envelope and HMA8 at the thylakoid membrane. To gain further insight into the way Cu is delivered to PC, we analysed the enzymatic properties of HMA8 and compared them with HMA6 ones using in vitro phosphorylation assays and phenotypic tests in yeast. These experiments reveal that HMA6 and HMA8 display different enzymatic properties: HMA8 has a higher apparent affinity for Cu + but a slower dephosphorylation kinetics than HMA6. Modelling experiments suggest that these differences could be explained by the electrostatic properties of the Cu + releasing cavities of the two transporters and/or by the different nature of their cognate Cu + acceptors (metallochaperone/PC). [ABSTRACT FROM AUTHOR]

Published
2015
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93. Analytical ultracentrifugation and preliminary X-ray studies of the chloroplast envelope quinone oxidoreductase homologue from Arabidopsis thaliana.

Author

Mas y mas, Sarah, Giustini, Cécile, Ferrer, Jean-Luc, Rolland, Norbert, Curien, Gilles, and Cobessi, David

Subjects
OXIDOREDUCTASES, ARABIDOPSIS thaliana, ULTRACENTRIFUGATION, CHLOROPLASTS, QUINONE, ESCHERICHIA coli
Abstract

Quinone oxidoreductases reduce a broad range of quinones and are widely distributed among living organisms. The chloroplast envelope quinone oxidoreductase homologue (ceQORH) from Arabidopsis thaliana binds NADPH, lacks a classical N-terminal and cleavable chloroplast transit peptide, and is transported through the chloroplast envelope membrane by an unknown alternative pathway without cleavage of its internal chloroplast targeting sequence. To unravel the fold of this targeting sequence and its substrate specificity, ceQORH from A. thaliana was overexpressed in Escherichia coli, purified and crystallized. Crystals of apo ceQORH were obtained and a complete data set was collected at 2.34 Å resolution. The crystals belonged to space group C2221, with two molecules in the asymmetric unit. [ABSTRACT FROM AUTHOR]

Published
2015
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96. HMA1, a New Cu-ATPase of the Chloro plast Envelope, Is Essential for Growth under Adverse Light Conditions

Author

Seigneurin-Berny, Daphné, primary, Gravot, Antoine, additional, Auroy, Pascaline, additional, Mazard, Christophe, additional, Kraut, Alexandra, additional, Finazzi, Giovanni, additional, Grunwald, Didier, additional, Rappaport, Fabrice, additional, Vavasseur, Alain, additional, Joyard, Jacques, additional, Richaud, Pierre, additional, and Rolland, Norbert, additional

Published
2006
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97. Evidence for a protein transported through the secretory pathway en route to the higher plant chloroplast

Author

Villarejo, Arsenio, primary, Burén, Stefan, additional, Larsson, Susanne, additional, Déjardin, Annabelle, additional, Monné, Magnus, additional, Rudhe, Charlotta, additional, Karlsson, Jan, additional, Jansson, Stefan, additional, Lerouge, Patrice, additional, Rolland, Norbert, additional, von Heijne, Gunnar, additional, Grebe, Markus, additional, Bako, Laszlo, additional, and Samuelsson, Göran, additional

Published
2005
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100. The hydrophobic proteome of mitochondrial membranes from Arabidopsis cell suspensions

Author

Brugière, Sabine, primary, Kowalski, Solène, additional, Ferro, Myriam, additional, Seigneurin-Berny, Daphné, additional, Miras, Stéphane, additional, Salvi, Daniel, additional, Ravanel, Stéphane, additional, d'Hérin, Pierre, additional, Garin, Jérôme, additional, Bourguignon, Jacques, additional, Joyard, Jacques, additional, and Rolland, Norbert, additional

Published
2004
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