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Accueil > Départements > Biochimie, Biophysique et Biologie Structurale > Solange MORERA : Microbiologie et enzymologie structurale



  • M. Kopečná, A. Vigouroux, J. Vilím, R. Končitíková, P. Briozzo, E. Hájková, L. Jašková, K. von Schwartzenberg, M. Šebela, S. Moréra, et D. Kopečný, « The ALDH21 gene found in lower plants and some vascular plants codes for a NADP(+) -dependent succinic semialdehyde dehydrogenase », The Plant Journal: For Cell and Molecular Biology, 2017.
    Résumé : Lower plant species including some green algae, non-vascular plants (bryophytes) as well as the oldest vascular plants (lycopods) and ferns (monilophytes) possess a unique aldehyde dehydrogenase (ALDH) gene named ALDH21, which is upregulated during dehydration. However, the gene is absent in flowering plants. Here, we show that ALDH21 from the moss Physcomitrella patens codes for a tetrameric NADP(+) -dependent succinic semialdehyde dehydrogenase (SSALDH), which converts succinic semialdehyde, an intermediate of the γ-aminobutyrate (GABA) shunt pathway, into succinate in the cytosol. NAD(+) is a very poor coenzyme for ALDH21 unlike for mitochondrial SSALDHs (ALDH5), which are the closest related ALDH members. Structural comparison between the apoform and the coenzyme complex reveal that NADP(+) binding induces a conformational change of the loop carrying Arg-228, which seals the NADP(+) in the coenzyme cavity via its 2'-phosphate and α-phosphate groups. The crystal structure with the bound product succinate shows that its carboxylate group establishes salt bridges with both Arg-121 and Arg-457 and a hydrogen bond with Tyr-296. While both arginine residues are pre-formed for substrate/product binding, Tyr-296 moves by more than 1 Å. Both R121A and R457A variants are almost inactive demonstrating a key role of each arginine in catalysis. Our study implies that bryophytes but presumably also some green algae, lycopods and ferns, which carry both ALDH21 and ALDH5 genes, can oxidize SSAL to succinate in both cytosol and mitochondria indicating more diverse GABA shunt pathway compared with higher plants carrying only the mitochondrial ALDH5. This article is protected by copyright. All rights reserved.
    Mots-clés : aldehyde dehydrogenase, ALDH21, ALDH5, B3S, GABA, MESB3S, Physcomitrella patens, site-directed mutagenesis, structure-function, succinic semialdehyde, x-ray crystallography.

  • J. Lang, A. Vigouroux, A. El Sahili, A. Kwasiborski, M. Aumont-Nicaise, Y. Dessaux, J. A. Shykoff, S. Moréra, et D. Faure, « Fitness costs restrict niche expansion by generalist niche-constructing pathogens », The ISME Journal, vol. 11, nᵒ 2, p. 374-385, 2017.
    Mots-clés : B3S, MESB3S, MICROBIO, PBI, PF, PIM.


  • L. Carles, P. Besse-Hoggan, M. Joly, A. Vigouroux, S. Morera, et I. Batisson, « Functional and structural characterization of two Bacillus megaterium nitroreductases biotransforming the herbicide mesotrione », Biochemical Journal, vol. 473, nᵒ 10, p. 1443-1453, mai 2016.

  • M. Cerezo, A. Lehraiki, A. Millet, F. Rouaud, M. Plaisant, E. Jaune, T. Botton, C. Ronco, P. Abbe, H. Amdouni, T. Passeron, V. Hofman, B. Mograbi, A. - S. Dabert-Gay, D. Debayle, D. Alcor, N. Rabhi, J. - S. Annicotte, L. Héliot, M. Gonzalez-Pisfil, C. Robert, S. Moréra, A. Vigouroux, P. Gual, M.  M. U. Ali, C. Bertolotto, P. Hofman, R. Ballotti, R. Benhida, et S. Rocchi, « Compounds Triggering ER Stress Exert Anti-Melanoma Effects and Overcome BRAF Inhibitor Resistance », Cancer Cell, vol. 30, nᵒ 1, p. 183, 2016.

  • C. Grandclément, M. Tannières, S. Moréra, Y. Dessaux, et D. Faure, « Quorum quenching: role in nature and applied developments », FEMS Microbiology Reviews, vol. 40, nᵒ 1, p. 86-116, 2016.
    Mots-clés : Acyl-Butyrolactones, acylase, Agrobacterium, amidase, anti-virulence, B3S, bacteria, Bacterial Physiological Phenomena, Biofilms, Chromobacterium, homoserine lactone, lactonase, MESB3S, MICROBIO, paraoxonase, PBI, Pseudomonas, Quorum Sensing, quorum-sensing inhibitors, Signal Transduction.

  • D. Kopečný, R. Končitíková, H. Popelka, P. Briozzo, A. Vigouroux, M. Kopečná, D. Zalabák, M. Šebela, J. Skopalová, I. Frébort, et S. Moréra, « Kinetic and structural investigation of the cytokinin oxidase/dehydrogenase active site », FEBS Journal, vol. 283, nᵒ 2, p. 361-377, 2016.

  • L. Marty, A. Vigouroux, M. Aumont-Nicaise, Y. Dessaux, D. Faure, et S. Moréra, « Structural Basis for High Specificity of Amadori Compound and Mannopine Opine Binding in Bacterial Pathogens », The Journal of Biological Chemistry, vol. 291, nᵒ 43, p. 22638-22649, 2016.
    Résumé : Agrobacterium tumefaciens pathogens genetically modify their host plants to drive the synthesis of opines in plant tumors. Opines are either sugar phosphodiesters or the products of condensed amino acids with ketoacids or sugars. They are Agrobacterium nutrients and imported into the bacterial cell via periplasmic-binding proteins (PBPs) and ABC-transporters. Mannopine, an opine from the mannityl-opine family, is synthesized from an intermediate named deoxy-fructosyl-glutamine (DFG), which is also an opine and abundant Amadori compound (a name used for any derivative of aminodeoxysugars) present in decaying plant materials. The PBP MotA is responsible for mannopine import in mannopine-assimilating agrobacteria. In the nopaline-opine type agrobacteria strain, SocA protein was proposed as a putative mannopine binding PBP, and AttC protein was annotated as a mannopine binding-like PBP. Structural data on mannityl-opine-PBP complexes is currently lacking. By combining affinity data with analysis of seven x-ray structures at high resolution, we investigated the molecular basis of MotA, SocA, and AttC interactions with mannopine and its DFG precursor. Our work demonstrates that AttC is not a mannopine-binding protein and reveals a specific binding pocket for DFG in SocA with an affinity in nanomolar range. Hence, mannopine would not be imported into nopaline-type agrobacteria strains. In contrast, MotA binds both mannopine and DFG. We thus defined one mannopine and two DFG binding signatures. Unlike mannopine-PBPs, selective DFG-PBPs are present in a wide diversity of bacteria, including Actinobacteria, α-,β-, and γ-proteobacteria, revealing a common role of this Amadori compound in pathogenic, symbiotic, and opportunistic bacteria.
    Mots-clés : ABC transporter, B3S, Crystal Structure, DFG, host-pathogen interaction, isothermal titration calorimetry (ITC), mannopine, MESB3S, opine, periplasmic binding protein, PF, PIM, plant pathogen, x-ray crystallography.

  • M. Redrejo-Rodríguez, A. Vigouroux, A. Mursalimov, I. Grin, D. Alili, Z. Koshenov, Z. Akishev, A. Maksimenko, A. K. Bissenbaev, B. T. Matkarimov, M. Saparbaev, A. A. Ishchenko, et S. Moréra, « Structural comparison of AP endonucleases from the exonuclease III family reveals new amino acid residues in human AP endonuclease 1 that are involved in incision of damaged DNA », Biochimie, vol. 128-129, p. 20-33, 2016.


  • A. El Sahili, A. Kwasiborski, N. Mothe, C. Velours, P. Legrand, S. Moréra, et D. Faure, « Natural Guided Genome Engineering Reveals Transcriptional Regulators Controlling Quorum-Sensing Signal Degradation », PLOS ONE, vol. 10, nᵒ 11, p. e0141718, nov. 2015.
    Mots-clés : 4-Butyrolactone, Amino Acid Sequence, Amino Acid Substitution, B3S, Bacterial Proteins, Carboxylic Ester Hydrolases, Circular Dichroism, Crystallography, X-Ray, Directed Molecular Evolution, Gene Expression Regulation, Bacterial, Homoserine, Lactones, MESB3S, MICROBIO, Molecular Sequence Data, Mutation, Mutation, Missense, PBI, PF, PIM, Point Mutation, Polymorphism, Single Nucleotide, Protein Conformation, Protein Folding, Quorum Sensing, Rhodococcus, Transcription Factors, Transcription, Genetic.

  • A. El Sahili, S. - Z. Li, J. Lang, C. Virus, S. Planamente, M. Ahmar, B. G. Guimaraes, M. Aumont-Nicaise, A. Vigouroux, L. Soulère, J. Reader, Y. Queneau, D. Faure, et S. Moréra, « A Pyranose-2-Phosphate Motif Is Responsible for Both Antibiotic Import and Quorum-Sensing Regulation in Agrobacterium tumefaciens », PLOS Pathogens, vol. 11, nᵒ 8, p. e1005071, août 2015.
    Mots-clés : Adenine Nucleotides, Agrobacterium tumefaciens, Anti-Bacterial Agents, ATP-Binding Cassette Transporters, B3S, Bacterial Proteins, Crystallography, X-Ray, MESB3S, MICROBIO, Molecular Sequence Data, PBI, Protein Conformation, Quorum Sensing, Sugar Phosphates.

  • R. Končitíková, A. Vigouroux, M. Kopečná, T. Andree, J. Bartoš, M. Šebela, S. Moréra, et D. Kopečný, « Role and structural characterization of plant aldehyde dehydrogenases from family 2 and family 7 », Biochemical Journal, vol. 468, nᵒ 1, p. 109-123, mai 2015.
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Publications avant 2015

Julien Lang#, Armelle Vigouroux#, Sara Planamente, Abbas El Sahili, Pauline Blin, Magali Aumont-Nicaise, Yves Dessaux, Solange Moréra*, Denis Faure (2014) Agrobacterium uses a unique ligand-binding mode for trapping opines and acquiring a competitive advantage in the niche construction on plant host. PLOS Pathogens.

Rothé B ; Saliou JM, Quinternet M, Back R ; Tiotiu D, Jacquemin C, Loegler C, Schlotter F, Pena V, Eckert K, Moréra S, Van Dorsselaer A, Branlant C ; Massenet S, Sanglier-Cianferan S, Manival X, Charpentier B (2014) Protein Hit1, a novel box C/D snoRNP assembly factor, controls cellular concentration of the scaffolding protein Rsa1 by direct interaction. NAR 42, 10731-47.

Kopecna M, Blaschke H, Kopecny D, Vigouroux A, Koncitikova R, Novak O, Kotland O, Strnad M, Moréra S*, von Schwartzenberg K. (2013) Structure and function of nucleoside hydrolases from Physcomitrella and maize catalyzing hydrolysis of purine, pyrimidine and cytokinin ribosides. Plant Physiol.163, 1568-1583.

Lang J, Planamente S, Mondy S, Dessaux Y, Moréra S, Faure D. (2013). Concerted transfer of the virulence Ti plasmid and companion At plasmid in the Agrobacterium tumefaciens-induced plant tumour. Microbiol. 90, 1178-89.

Régis Back, Cyril Dominguez, Benjamin Rothé, Claude Bobo, Chrystel Beaufils, Solange Moréra, Philippe Meyer, Bruno Charpentier, Christiane Branlant, Frédéric H.-T. Allain, Xavier Manival (2013). NMR high resolution structures of free Tah1 and Tah1 bound to the Hsp90 C-terminal tail explains how Hsp90 recognizes the R2TP complex. Structure 2, 1834-1847.

Jakub Gruszczyk, Vanesa Olivares-Illana, Julien Nourikyan, Aurore Fleurie, Emmanuelle Béchet, Virginie Gueguen-Chaignon, Céline Freton, Magali Aumont-Nicaise, Solange Moréra, Christophe Grangeasse and Sylvie Nessler (2013). Comparative Analysis of the Tyr-Kinases CapB1 and CapB2 fused to their Cognate Modulators CapA1 and CapA2 from Staphylococcus aureus. PLOS one 8:e75958.

Abdelghani Mazouzi, Armelle Vigouroux, Bulat Aikeshev, Philip J. Brooks, Murat Saparbaev, Solange Morera*, Alexander A. Ishchenko (2013). Insight into mechanisms of 3’-5’ exonuclease activity and removal of bulky 8,5’-cyclopurine adducts by AP endonucleases. PNAS 110, E3071-3080.

Sara Planamente, Solange Morera*, Denis Faure (2013) In planta fitness-cost of the Atu4232-regulon encoding for a selective GABA-binding sensor in Agrobacterium. Commun Integr Biol. 1 ;6(3):e23692.

Kopečny D, Končitíková R, Tylichová M, Vigouroux A, Moskalíková H, Soural M, Šebela M, Moréra S.* (2013) Plant ALDH10 family : identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate. J Biol Chem. 288, 9491-507.

Tannières M, Beury-Cirou A, Vigouroux A, Mondy S, Pellissier F, Dessaux Y, Faure D. (2013) A Metagenomic Study Highlights Phylogenetic Proximity of Quorum-Quenching and Xenobiotic-Degrading Amidases of the AS-Family. PLoS One. 8:e65473

Sara Planamente, Samuel Mondy, Florence Hommais, Armelle Vigouroux, Solange Moréra*, Denis Faure (2012). Structural basis for selective GABA-binding in bacterial pathogens. Mol. Microbiol. 86, 1085-1099.

Tarang Khare, Shraddha Pai, Karolis Koncevicius, Mrinal Pal, Edita Kriukiene, Zita Liutkeviciute, Manuel Irimia, Peixin Jia, Carolyn Ptak, Menghang Xia, Raymond Tice, Mamoru Tochigi, Solange Moréra, Anaies Nazarians, Denise Belsham, Albert H C Wong, Benjamin J Blencowe, Sun Chong Wang, Philipp Kapranov, Rafal Kustra, Viviane Labrie, Saulius Klimasauskas & Arturas Petronis (2012). 5-hmC in the brain is abundant in synaptic genes and shows differences at the exon-intron boundary. NSMB. 19, 1037-1043.

Moréra* S, Inga Grin, Armelle Vigouroux, Sophie Couvé, Véronique Henriot, Murat Saparbaev and Alexander A. Ishchenko (2012). Biochemical and structural characterization of the glycosylase domain of MBD4 bound to thymine and 5-hydroxymethyuracil (5hmU)-containing DNA. Nucleic Acids Res 40, 9917-9926.

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