Biography
of Dr. Gilles Curien


Gilles Curien

Born on the 7th november 1969
Researcher (CR1) at the CNRS (France) since 2001

Laboratoire Physiologie Cellulaire & Végétale
iRTSV CEA-Grenoble
17 avenue des Martyrs, 38 054 Grenoble cedex 09, France
Phone: 33 4 38 78 66 63
Fax: 33 4 4 38 78 50 91

Grenoble / DSV, Center : BIG / PCV / LPM

Area of interest

I’m a biochemist and enzymologist interested in the dynamics of metabolic fluxes and energy regulation in photosynthetic organisms (plant, algae’s). Living systems have evolved sophisticated molecular mechanis​ms to prevent shortage or over-accumulation of metabolites upon variation in the environmental conditions and I specifically focus my attention on integrated short-term controls occurring in a matter of minutes [1]. A thorough understanding of the function of molecular mechanisms described in vitro requires the integration of biochemical data into quantitative mathematical models to carry out simulations.

Another challenge in metabolism is the representation of the wealth of molecular data accumulated for more than 50 years of research into a comprehensive whole. The extreme imbrication of the processes results in an i​mpossibility for the human mind to capture metabolism behaviour at a single glance. To overcome this caveat I’m involved in the development of a specific visual Web Interface to explore the metabolism of the model photosynthetic organism A. thaliana at the molecular level (in collaboration with the EDyP team (BGE laboratory at our institute, CEA-Grenoble) for the bioinformatics and with team D-Phy-Chloro, and team Dynamic of C1 metabolism in our laboratory). This friendly visual web interface (soon available to the public) will facilitate research communication, generation of hypotheses, knowledge acquisition by students, and will help biotechnologists to rationally choose target enzymes to knock-out or overproduce.

[1]Stocks of metabolites are generally small (1-10 million molecules in a chloroplast for example) compared to the fluxes for their transformation (1-10 million per seconds for the fastest processes). In the absence of efficient and fast regulatory processes (operating in a matter of seconds) oscillations and chaotic behaviour would be encountered by living systems, limiting growth (shortage) or leading to death (over-accumulation of toxic metabolic intermediates).

PROFILE

  • 2014
    Habilitation à diriger des recherches
    (HDR, Univ Grenoble Alpes)
  • 2001
    Permanent position at the CNRS
  • 1999/2000
    Human Frontier Post Doctoral Fellowship
    University of Marylands (USA). Host: Pr George Lorimer.
  • 1995/1998
    PhD Thesis. Allosteric activation of plant Threonine synthase
    University Joseph Fourier (Grenoble).
  • 1994/1995
    Master 2 in Molecular and Cellular Biology
    University Joseph Fourier-ENS Lyon
  • 1990/1992
    Master
    (Molecular and Cellular Biology-Ecole Normale Supérieure Lyon)
  • 1993
    Agrégation de biochimie
  • 1987/1990
    Classes préparatoires Mathématiques Supérieures Biologie (Metz)

Publications

Mas Y Mas S, Giustini C, Ferrer JL, Rolland N, Curien G and Cobessi D
Analytical ultracentrifugation and preliminary X-ray studies of the chloroplast envelope quinone oxidoreductase homologue from Arabidopsis thaliana.
Acta Crystallographica, Section F Structural Biology Communications, 2015, 71(Pt 4): 455-458

Curien G*, Cárdenas ML and Cornish-Bowden A
Analytical kinetic modeling: A practical procedure.
Methods in Molecular Biology, 2014, 1090: 261-280

Graindorge M, Giustini C, Kraut A, Moyet L, Curien G and Matringe M
Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms.
Journal of Biological Chemistry, 2014, 289(6): 3198-3208

Dell'aglio E, Giustini C, Salvi D, Brugiere S, Delpierre F, Moyet L, Baudet M, Seigneurin-Berny D, Matringe M, Ferro M, Rolland N and Curien G
Complementary biochemical approaches applied to the identification of plastidial calmodulin-binding proteins.
Molecular BioSystems, 2013, 9(6): 1234-1248

Dumas R, Cobessi D, Robin AY, Ferrer JL and Curien G
The many faces of aspartate kinases.
Archives of Biochemistry and Biophysics, 2012, 519(2): 186–193

Rolland N, Curien G, Finazzi G, Kuntz M, Maréchal E, Matringe M, Ravanel S and Seigneurin-Berny D
The biosynthetic capacities of the plastids and integration between cytoplasmic and chloroplast processes.
Annual Review of Genetics, 2012, 46: 233-264

Curien G, Dumas R, Cornish-Bowden A and Cárdenas M
Different contributions of the various isoenzymes to the flux in the aspartate-derived amino acid pathway in Arabidopsis thaliana.
Experimental Standard Conditions of Enzyme Characterizations III (ed. M. G. Hicks & C. Kettner) Beilstein Institute, Frankfurt. 2011

Graindorge M, Giustini C, Jacomin AC, Kraut A, Curien G* and Matringe M
Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: The last homeless enzyme of aromatic amino acids biosynthesis.
Febs Letters, 2010, 584(20): 4357-4360

Robin A, Cobessi D, Curien G, Robert-Genthon M, Ferrer J-L and Dumas R
A new mode of dimerization of allosteric enzymes with ACT domains revealed by the crystal structure of the aspartate kinase from Cyanobacteria.
Journal of Molecular Biology, 2010, 399(2): 283-293

Curien G*, Bastien O, Robert-Genthon M, Cornish-Bowden A, Cardenas ML and Dumas R
Understanding regulation of aspartate metabolism with a model based on measured kinetic parameters.
Molecular Systems Biology, 2009, 5: 271

Benamar A, Rolletschek H, Borisjuk L, Avelange-Macherel MH, Curien G, Mostefai HA, Andriantsitohaina R and Macherel D
Nitrite-nitric oxide control of mitochondrial respiration at the frontier of anoxia.
Biochimical and Biophysica Acta-Bioenergetics, 2008, 1777(10): 1268-1275

Curien G, Biou V, Mas-Droux C, Robert-Genthon M, Ferrer JL and Dumas R
Amino acid biosynthesis: New architectures in allosteric enzymes.
Plant Physiology and Biochemistry, 2008, 46(3): 325-339

Curien G*, Laurencin M, Robert-Genthon M and Dumas R
Allosteric monofunctional aspartate kinases from Arabidopsis.
FEBS Journal, 2007, 274(1): 164-176

Mas-Droux C, Curien G, Robert-Genthon M, Laurencin M, Ferrer JL and Dumas R
A novel organization of ACT domains in allosteric enzymes revealed by the crystal structure of Arabidopsis Aspartate kinase.
Plant Cell, 2006, 18(7): 1681-1692

Fiévet JB, Dillmann C, Curien G and de Vienne D
Simplified modelling of metabolic pathways for flux prediction and optimization: Lessons from an in vitro reconstruction of the upper part of glycolysis.
Biochemical Journal, 2006, 396(2): 317-326

Curien G*, Ravanel S, Robert M and Dumas R
Identification of six novel Allosteric effectors of Arabidopsis thaliana Aspartate kinase-Homoserine dehydrogenase isoforms: Physiological context sets the specificity.
Journal of Biological Chemistry, 2005, 280(50): 41178-41183

Ravanel S, Block MA, Rippert P, Jabrin S, Curien G, Rébeillé F and Douce R
Methionine metabolism in plants: Chloroplasts are autonomous for de novo methionine synthesis and can import S-adenosylmethionine from the cytosol.
Journal of Biological Chemistry, 2004, 279(21): 22548-22557

Curien G*, Ravanel S and Dumas R
A kinetic model of the branch-point between the methionine and threonine biosynthesis pathways in Arabidopsis thaliana.
European Journal of Biochemistry, 2003, 270(23): 4615-27

Paris S, Viemon C, Curien G and Dumas R
Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine.
Journal of Biological Chemistry, 2003, 278(7): 5361-5366

Thomazeau K, Curien G, Dumas R and Biou V
Crystal structure of threonine synthase from Arabidopsis thaliana.
Protein Science, 2001, 10(3): 638-648

Thomazeau K, Curien G, Thompson A, Dumas R and Biou V
MAD on threonine synthase: The phasing power of oxidized selenomethionine.
Acta Crystallographica. Section D, Biological Crystallography, 2001, 57(Part 9): 1337-1340

Aubert S, Curien G, Bligny R, Gout E and Douce R
Transport, compartmentation, and metabolism of homoserine in higher plant cells. Carbon-13- and phosphorus-31-nuclear magnetic resonance studies.
Plant Physiology, 1998, 116(2): 547-557

Curien G*, Job D, Douce R and Dumas R
Allosteric activation of Arabidopsis threonine synthase by S-adenosylmethionine.
Biochemistry, 1998, 37(38): 13212-13221

Curien G, Dumas R, Ravanel S and Douce R
Characterization of an Arabidopsis thaliana cDNA encoding an S-adenosylmethionine-sensitive threonine synthase. Threonine synthase from higher plants.
FEBS Letters, 1996, 390(1): 85-90

Curien G, Dumas R and Douce R
Nucleotide sequence and characterization of a cDNA encoding the acetohydroxy acid isomeroreductase from Arabidopsis thaliana.
Plant Molecular Biology, 1993, 21(4): 717-722

Dumas R, Curien G, DeRose R and Douce R
Branched-chain-amino-acid biosynthesis in plants: Molecular cloning and characterization of the gene encoding acetohydroxy acid isomeroreductase (ketol-acid reductoisomerase) from Arabidopsis thaliana (thale cress).
Biochemical Journal, 1993, 294(Pt 3): 821-828

*corresponding author